Kumari R, Ven K, Chastney M, Kokate SB, Peränen J, Aaron J, Almeida-Souza L, Kremneva E, Poincloux R, Chew T-L, Gunning PW, Ivaska J, Lappalainen P (2024): Focal adhesions contain three specialized actin nanoscale layers. Nat. Commun. (in press).
*Vizcaíno-Castillo A, *Kotila T, *Kogan K, *Yanase R, Como J, Antenucci L, Michelot A, Sunter JC, Lappalainen P (2024): Unusual actin-binding mechanism and the role of profilin in actin dynamics of trypanosomatid parasites. J. Biol. Chem. (in press) *equal contribution
Vasilescu C, Colpan M, Ojala TH, Manninen T, Mutka A, Ylänen K, Rahkonen O, Poutanen T, Martelius L, Kumari R, Hinterding H, Brilhante V, Ojanen S, Lappalainen P, Koskenvuo J, Carroll CJ, Fowler VM, Gregorio CC, Suomalainen A. (2024): Recessive TMOD1 mutation causes childhood cardiomyopathy. Commun. Biol. 7(1): 7. doi.org/10.1038/s42003-023-05670-9
Zhang Y, Zhang X, Li Z, Zhao W, Yang H, Zhao S, Tang D, Zhang Q, Li Z, Liu H, Li H, Li B, Lappalainen P, Xu T, Cui Z, Jiu Y (2023): Single particle tracking reveals SARS-CoV-2 regulating and utilizing dynamic filopodia for viral invasion. Sci. Bull. 68(19): 2210-2224. doi.org/10.1016/j.scib.2023.08.031
Selvaraj M*, Kokate SB*, Reggiano G, Kogan K, Kotila T, Kremneva E, DiMaio F, Lappalainen P, Huiskonen JT (2023): Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms. Cell Reports 42: 111900. doi.org/10.1016/j.celrep.2022.111900. *equal contribution.
Senju Y, Mushtaq T, Helena Vihinen H, Manninen A, Saarikangas J, Ven K, Engel U, Varjosalo M, Jokitalo E, Lappalainen P (2023): Actin-rich lamellipodia-like protrusions contribute to the integrity of epithelial cell–cell junctions. J Biol. Chem. 299: 104571. doi.org/10.1016/j.jbc.2023.104571
Colin A, Kotila T, Guérin C, Orhant-Prioux M, Vianay B, Mogilner A, Lappalainen P, Théry M, Blanchoin L (2023): Recycling limits the lifetime of actin turnover. EMBO J. e112717. doi.org/10.15252/embj.2022112717
Kokate SB, Ciuba K, Tran VD, Kumari R, Tojkander S, Engel U, Kogan K, Kumar S, Lappalainen P (2022): Caldesmon controls stress fiber force-balance through dynamic cross-linking of myosin II and actin-tropomyosin filaments. Nat Commun. 13: 6032. doi.org/10.1038/s41467-022-33688-w
Tsai F-C, Henderson JM, Jarin Z, Kremneva E, Senju Y, Pernier J, Mikhajlov O, Manzi J, Kogan K, Le Clainche C, Voth GA, Lappalainen P, Bassereau P (2022): Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions. Sci. Adv. 8(41). doi.org/10.1126/sciadv.abp8677
Kotila T, Wioland H, Muniyandi S, Kogan K, Antenucci L, Jégou A, Huiskonen J, Romet-Lemonne G, Lappalainen P (2022): Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite. Nat. Commun. 13: 3442. doi: 10.1038/s41467-022-31068-y
Lappalainen P. Kotila T, Jegou A, Romet-Lemonne G. (2022): Biochemical and mechanical regulation of actin dynamics. Nat. Rev. Mol. Cell Biol. doi: 10.1038/s41580-022-00508-4
Kogan K, Haapasalo K, Kotila T, Moore R, Lappalainen P, Goldman A, Meri T (2022): Mechanism of Borrelia immune evasion by FhbA-related proteins. PLoS Pathogens 18(3):e1010338. doi: 10.1371/journal.ppat.1010338
Lechuga S, Cartagena-Rivera AX, Khan A, Crawford BI, Narayanan V, Conway DE, Lehtimäki J, Lappalainen P, Rieder F, Longworth MS, Ivanov AI. (2022): A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair. FASEB J. 36(5):e22290. doi: 10.1096/fj.202200154R
Salomaa SI, Miihkinen M, Kremneva E, Paatero I, Lilja J, Jacquemet G, Vuorio J, Antenucci L, Kogan K, Nia FH, Hollos P, Isomursu A, Vattulainen I, Coffey ET, Kreienkamp H-J, Lappalainen P, Ivaska J. SHANK3 conformation regulates direct actin binding and crosstalk with Rap1 signaling. Curr. Biol. 31(22):4956-4970.e9 . doi: 10.1016/j.cub.2021.09.022
Lehtimäki JI, Rajakylä EK, Tojkander S, Lappalainen P. Generation of stress fibers through myosin-driven re-organization of the actin cortex. eLife 10:e60710. doi: 10.7554/eLife.60710.
Hakala M, Wioland H, Tolonen M, Kotila T, Jegou A, Romet-Lemonne G, Lappalainen P. Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks. Nature Cell Biol. 23: 147-159. doi: 10.1038/s41556-020-00629-y.
Colombo J, Antkowiak A, Kogan K, Kotila T, Elliott J, Guillotin A, Lappalainen P, Michelot A . A functional family of fluorescent nucleotide analogues to investigate actin dynamics and energetics. Nature Commun. 12:548. doi: 10.1038/s41467-020-20827-4.
Mäkitie RE, Henning P, Jiu Y, Kämpe A, Kogan K, Costantini A, Välimäki VV, Medina-Gomez C, Pekkinen M, Salusky IB, Schalin-Jäntti C, Haanpää MK, Rivadeneira F, Bassett JHD, Williams GR, Lerner UH, Pereira RC, Lappalainen P, Mäkitie O. An ARHGAP25 variant links aberrant Rac1 function to early-onset skeletal fragility. JBMR Plus. doi: 10.1002/jbm4.10509.
Inamdar K, Tsai FC, Dibsy R, de Poret A, Manzi J, Merida P, Muller R, Lappalainen P, Roingeard P, Mak J, Bassereau P, Favard C, Muriaux DM. Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53. eLife 10:e67321. doi: 10.7554/eLife.67321.
Senju Y, Lappalainen P, Zhao H. Liposome Co-sedimentation and Co-flotation Assays to Study Lipid-Protein Interactions. Methods Mol. Biol. 2251:195-204. (Book chapter). doi: 10.1007/978-1-0716-1142-5_14.
Coulombe PA, Lappalainen P. Editorial: Architectural cell elements as multimodal sensors, transducers, and actuators. Curr. Opin. Cell Biol. S0955-0674(20)30170-8. (Editorial). doi: 10.1016/j.ceb.2020.12.005.
Kumari R, Jiu Y, Carman PJ, Tojkander S. Kogan K, Varjosalo M, Gunning PW, Dominguez R, Lappalainen P. Tropomodulins control the balance between protrusive and contractile structures by stabilizing actin-tropomyosin filaments. Curr. Biol. 30: 767–778. doi: 10.1016/j.cub.2019.12.049.
Rajakylä K, Lehtimäki J, Acheva A, Schaible N, Lappalainen P, Krishnan R, Tojkander S. Assembly of peripheral actomyosin bundles in epithelial cells is dependent on CaMKK2/AMPK pathway. Cell Reports 30: 4266-4280.e4. doi: 10.1016/j.celrep.2020.02.096.
Becker IC, Scheller I, Wackerbarth LM, Beck S, Heib T, Aurbach K, Manukjan G, Gross C, Spindler M, Nagy Z, Witke W, Lappalainen P, Bender M, Schulze H, Pleines I, Nieswandt B (2020): Actin/microtubule crosstalk during platelet biogenesis in mice is critically regulated by Twinfilin1 and Cofilin1. Blood Adv. 4: 2124-2134. doi: 10.1182/bloodadvances.2019001303.
Kotila T, Wioland H, Enkavi G, Kogan K, Vattulainen I, Jégou A, Romet-Lemonne G, Lappalainen P. Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Nature Commun. 10:5320. doi: 10.1038/s41467-019-13213-2.
Lappalainen P. Protein modification fine-tunes the cell's force producers. Nature. 2019 Jan 565(7739):297-298. doi: 10.1038/d41586-018-07882-0.
Senju Y, Lappalainen P. Regulation of actin dynamics by PI(4,5)P2 in cell migration and endocytosis. Curr Opin Cell Biol. 2019 Feb;56:7-13. Epub 2018 Sep 5. doi: 10.1016/j.ceb.2018.08.003.
Jiu Y, Kumari R, Fenix AM, Schaible N, Liu X, Varjosalo M, Krishnan R, Burnette DT, Lappalainen P. Myosin-18B promotes the assembly of myosin II stacks for maturation of contractile actomyosin bundles. Curr Biol. 2019 Jan 7;29(1):81-92.e5. doi: 10.1016/j.cub.2018.11.045. Epub 2018 Dec 20.
Ciuba K, Hawkes W, Tojkander S, Kogan K, Engel U, Iskratsch T, Lappalainen P. Calponin-3 is critical for coordinated contractility of actin stress fibers. Sci. Reports. ;Dec 5;8(1):17670. doi: 10.1038/s41598-018-35948-6.
Tsai FC, Bertin A, Bousquet H, Manzi J, Senju Y, Picas L, Miserey-Lenkei S, Lappalainen P, Lemichez E, Coudrier E, Bassereau P. Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner. Elife. 2018 Sep 20;7. pii: e37262. doi: 10.7554/eLife.37262.
Tojkander S, Ciuba K, Lappalainen P. CaMKK2 regulates mechanosensitive assembly of contractile actin stress fibers. Cell Reports 24: 11-19. doi: 10.1016/j.celrep.2018.06.011.
*Kotila T, *Kogan K, Enkavi G, Guo S, Vattulainen I, Goode BL, Lappalainen P.Structural basis of actin monomer re-charging by cyclase-associated protein. Nature Commun. 9:1892. doi: 10.1038/s41467-018-04231-7.*equal contribution.
Hakala M, Kalimeri M, Enkavi G, Vattulainen I, Lappalainen P. Molecular mechanism for inhibition of twinfilin by phosphoinositides. J Biol. Chem. 293: 4818-4829. doi: 10.1074/jbc.RA117.000484.
Senju Y, Kalimeri M, Koskela EV, Somerharju P, Zhao H, Vattulainen I, Lappalainen P. Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides. Proc. Natl. Acad. Sci. 114: E8977-E8986. doi:10.1073/pnas.1705032114.
Lehtimäki JI, Fenix AM, Kotila T, Balistreri G, Paavolainen L, Varjosalo M, Burnette BT, Lappalainen P. UNC-45a promotes myosin folding and stress fiber assembly. J Cell Biol. 216: 4053-4072. doi:10.1083/jcb.201703107.
Stritt S, Beck S, Becker IC, Vogtle T, Hakala M, Heinze KG, Du X, Bender M, Braun A, Lappalainen P, Nieswandt B. Twinfilin 2a is a regulator of platelet reactivity and turnover in mice. Blood. 130: 1746-1756. doi:10.1182/blood-2017-02-770768.
Khan MH, Salomaa SI, Jacquemet G, Butt U, Miihkinen M, Deguchi T, Kremneva E, Lappalainen P, Humphries MJ, Pouwels J. The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex. J Cell Sci. 130: 3094-3107. doi:10.1242/jcs.200329.
Wioland H, Guichard B, Senju Y, Myram S, Lappalainen P, Jegou A, Romet-Lemonne G. ADF/cofilin accelerates actin dynamics by severing filaments and promoting their depolymerization at both ends. Curr. Biol. 27: 1956-1967. doi:10.1016/j.cub.2017.05.048.
Stefani C, Gonzalez-Rodriguez D, Senju Y, Doye A, Efimova N, Janel S, Lipuna J, Tsai MC, Hamaoui D, Maddugoda M, Cochet-Escartin O, Prevost C, Lafont F, Svitkina T, Lappalainen P, Bassereau P, Lemichez E. Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation. Nat. Commun. 8:15839. doi:10.1038/ncomms15839.
Gateva G, Kremneva E, Reindl T, Kotila T, Kogan K, Gressin L, Gunning PW, Manstein DJ, Michelot A, Lappalainen P. Tropomyosin isoforms specify functionally distinct actin filament populations in vitro. Curr. Biol. 27, 705-713. doi:10.1016/j.cub.2017.01.018.
Pfisterer S, Gateva G, Horvath P, Pirhonen J, Salo V, Karhinen L, Varjosalo M, Ryhänen S, Lappalainen P, Ikonen E. Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage. Nature Commun. 8:14858. doi:10.1038/ncomms14858.
Jiu Y, Peränen J, Schaible N, Cheng F, Eriksson JE, Krishnan R, Lappalainen P. Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA. J Cell Sci. 130: 892-902. doi:10.1242/jcs.196881.
Lehtimäki J, Hakala M, Lappalainen P. Actin Filament Structures in Migrating Cells. Handb Exp Pharmacology235:123-152. doi:10.1007/164_2016_28.
Lappalainen P. Actin-binding proteins: the long road to understanding the dynamic landscape of cellular actin networks. Mol Biol Cell.,27:2519-2522. doi:10.1091/mbc.E15-10-0728.
Tojkander S, Gateva G, Husain A, Krishnan R, Lappalainen P. Generation of contractile actomyosin bundles depends on mechanosensitive actin filament assembly and disassembly. eLife, 4:e06126. doi:10.7554/eLife.06126.
Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R. How leiomodin and tropomodulin use a common fold for different actin assembly functions. Nat. Commun. 15;6:8314. doi:10.1038/ncomms9314.
Prévost C, Zhao H, Manzi J, Lemichez E, Lappalainen P, Callan-Jones A,; Bassereau P. IRSp53 senses negative membrane curvature and phase separates along membrane tubules. Nat. Commun. 15:6:8529. doi:10.1038/ncomms9529
Gunning PW, Hardeman EC, Lappalainen P, Mulvihill DP. Tropomyosin: Master regulator of actin filament function in the cytoskeleton. J. Cell Sci. 128: 2965-74. doi:10.1242/jcs.172502.
Jiu Y, Lehtimäki J, Tojkander S, Cheng F, Jäälinoja H, Liu X, Varjosalo M, Eriksson JE, Lappalainen P. Bidirectional interplay between vimentin intermediate filaments and contractile actin stress fibers. Cell Reports 11: 1511-1518. doi:10.1016/j.celrep.2015.05.008.
Saarikangas J, Kourdougli N, Senju Y, Chazal G, Segerstråle M, Minkeviciene R, Kuurne J, Mattila PK, Garrett L, Hölter SM, Becker L, Racz I, Hans W, Klopstock T, Wurst W, Zimmer A, Fuchs H, Gailus-Durner V, Hrabě de Angelis M, von Ossowski L, Taira T, Lappalainen P, Rivera C, Hotulainen P. MIM-induced membrane bending promotes dendritic spine initiation. Dev. Cell 33: 644-659. doi:10.1016/j.devcel.2015.04.014.
Poukkula M, Hakala M, Pentinmikko N, Sweeney MO, Jansen S, Mattila J, Hietakangas V, Goode BL, Lappalainen P. GMF promotes leading edge dynamics and collective cell migration in vivo. Curr. Biol. 24: 2533-2540. doi:10.1016/j.cub.2014.08.066.
Kremneva E, Makkonen MH, Skwarek-Maruszewska A, Gateva G, Michelot A, Dominguez R, Lappalainen P. Cofilin-2 controls actin filament length in muscle sarcomeres. Dev. Cell. 31: 215-226. doi:10.1016/j.devcel.2014.09.002.
Kostan J, Salzer U, Orlova A, Törö I, Hodnik V, Senju Y, Zou J, Schreiner C, Steiner J, Meriläinen J, Nikki M, Virtanen I, Carugo O, Rappsilber J, Lappalainen P, Lehto V-P, Anderluh G, Egelman EH, Djinović-Carugo K. Direct interaction of actin filaments with F-BAR protein pacsin2. EMBO Rep. 15: 1154-1162. doi:10.15252/embr.201439267.
Gateva G, Tojkander S, Koho S, Carpen O, Lappalainen P. Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment. J. Cell Sci. 127: 1887-98. doi:10.1242/jcs.135780.
Mertz KD, Pathria G, Wagner C, Saarikangas J, Sboner A, Romanov J, Gschaider M, Lenz F, Neumann F, Schreiner W, Nemethova M, Glassmann A, Lappalainen P, Stingl G, Small JV, Fink D, Chin L, Wagner SN. MTSS1 is a metastasis driver in a subset of human melanomas. Nat. Commun. 5:3465. doi:10.1038/ncomms4465.
Talma V., Gateva G., Ekokoski E, Lappalainen P, Tuominen RK. Evidence for a role of MRCK in mediating HeLa cell elongation induced by the C1 domain ligand HMI-1a3. Eur. J. Pharm. Sci. 55: 46-57. doi:10.1016/j.ejps.2014.01.002.
Linkner J, Witte G, Zhao H, Junemann A, Nordholz B, Runge-Wollmann P, Lappalainen P, Faix J. The inverse BAR-domain protein IBARa drives membrane remodelling to control osmoregulation, phagocytosis and cytokinesis. J. Cell Sci. 127: 1279-1292. doi:10.1242/jcs.140756.
Kanerva K, Uronen R, Blom T, Li S, Bittman R, Lappalainen P, Peränen J, Raposo G, Ikonen E. LDL-cholesterol is recycled to the plasma membrane via Rab8a-Myosin5b-actin dependent membrane transport. Dev. Cell 27: 249-262. doi:10.1371/journal.pone.0029385.
Zhao H, Michelot A, Koskela EV, Tkach V, Stamou D, Drubin DG, Lappalainen P. Memebrane-sculptingBin-Amphiphysin-Rvs (BAR) domains generate stable lipid microdomains. Cell Reports 6: 1213-1223. doi:10.1016/j.celrep.2013.08.024.
Makkonen M, Bertling E, Chebotareva NA, Baum J, Lappalainen P. Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism. J. Biol. Chem. 288: 984-994. doi:10.1074/jbc.M112.435719.
Pivovarova AV, Chebotareva NA, Kremneva EV, Lappalainen P, Levitsky DI. Effects of Actin-Binding Proteins on the Thermal Stability of Monomeric Actin. Biochemistry 52: 152-160. doi:10.1021/bi3012884.
Weber-Boyvat M, Zhao H, Aro N, Yuan Q, Chernov K, Peränen J, Lappalainen P, Jäntti J. A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions. Mol. Biol. Cell 24: 331-341. doi:10.1091/mbc.E12-05-0415.
Lehtonen HJ, Sipponen T, Tojkander S, Karikoski R, Järvinen H, Laing NG, Lappalainen P, Aaltonen LA, Tuupanen S. Segregation of a Missense Variant in Enteric Smooth Muscle Actin γ-2 with Autosomal Dominant Familial Visceral Myopathy. Gastroenterology. 143:1482-1491. doi:10.1053/j.gastro.2012.08.045.
Zhao H, Lappalainen P. A simple guide to biochemical approaches for analyzing protein-lipid interaction. Mol Biol Cell. 23(15):2823-30. doi:10.1091/mbc.E11-07-0645.
Kotiadis V, Leadsham J, Bastow E, Gheeraert A, Whybrew J, Bard M, Lappalainen P, Gourlay C. Identification of new surfaces of cofilin that link mitochondrial function to the control of multi-drug resistance. J. Cell Sci. ;125:2288-2299. doi:10.1242/jcs.099390.
Tojkander S, Gateva G, Lappalainen P. Actin stress fibers - assembly, dynamics and biological roles. J. Cell Sci. 125:1855-1864. doi:10.1242/jcs.098087.
Maddugoda MP, Stefani C, Gonzalez-Rodriguez D, Saarikangas J, Torrino S, Janel S, Prodon F, Doye A, Goossens PL, Lafont F, Bassereau P, Lappalainen P, Brochard F, Lemichez E. cAMP signaling by Anthrax edema toxin induces transendothelial cell tunnels, which are resealed by MIM via Arp2/3-driven actin polymerization. Cell Host & Microbe 10:464-474. doi:10.1016/j.chom.2011.09.014.
Nevalainen EM, Braun A, Vartiainen MK, Serlachius M, Andersson LC, Moser M, Lappalainen P. Twinfilin-2a is dispensable for mouse development. PLoS One. 2011;6(8):e22894. Epub 2011 Aug 18. doi:10.1371/journal.pone.0022894.
Poukkula M, Kremneva E, Serlachius M, Lappalainen P. Actin-depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton (Hoboken). 68:471-490. doi:10.1002/cm.20530.
Pykäläinen A, Boczkowska M, Zhao H, Saarikangas J, Rebowski G, Jansen; M, Hakanen J,; Koskela; E V, Peränen J, Vihinen H, Jokitalo E, Salminen; M, Ikonen E, Dominguez R, Lappalainen P. Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures. Nat Struct Mol Biol. 18:902-907. doi:10.1038/nsmb.2079.
Tojkander S, Gateva G, Schevzov G, Hotulainen P, Naumanen P, Martin C, Gunning PW, Lappalainen P. A Molecular Pathway for Myosin II Recruitment to Stress Fibers. Current Biology. 21:539-550. doi:10.1016/j.cub.2011.03.007.
Saarikangas J, Mattila PK, Varjosalo M, Bovellan M, Hakanen J, Calzada-Wack J, Tost M, Jennen L, Rathkolb B, Hans W, Horsch M, Hyvönen ME, Perälä N, Fuchs H, Gailus-Durner V, Esposito I, Wolf E, de Angelis MH, Frilander MJ, Savilahti H, Sariola H, Sainio K, Lehtonen S, Taipale J, Salminen M, Lappalainen P.Missing-in-metastasis MIM/MTSS1 promotes actin assembly at intercellular junctions and is required for integrity of kidney epithilia. J Cell Sci. 124:1245-1255. doi:10.1242/jcs.082610.
Zhao H, Pykäläinen A, Lappalainen P. I-BAR domain proteins: linking actin and plasma membrane dynamics. Curr Opin Cell Biol. 23:14-21. doi:10.1016/j.ceb.2010.10.005.
Skwarek-Maruszewska A, Boczkowska M, Zajac AL, Kremneva E, Svitkina T, Dominguez R, Lappalainen P. Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeres. Mol. Biol. Cell. 21:3352-3361. doi:10.1091/mbc.E10-02-0109.
Ramalingam N, Zhao H, Breitsprecher D, Lappalainen P, Faix J, Schleicher M. Phospholipids regulate localization and activity of mDia1 formin. Eur. J. Cell Biol. 89:723-732. doi:10.1016/j.ejcb.2010.06.001.
Saarikangas J , Zhao H , Lappalainen P. Regulation of the interplay between the actin cytoskeleton and plasma membrane by phosphpinositides. Physiol. Rev. 90: 259-289. doi:10.1152/physrev.00036.2009.
Gandhi M, Smith BA, Bovellan M , Paavilainen V , Daugherty-Clarke K, Gelles J, Lappalainen P , Goode BL. GMF is a cofilin homologue that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation. Curr. Biol. 20: 861-867. doi:10.1016/j.cub.2010.03.026.
Zhao H , Hakala M , Lappalainen P. ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP 2 -density sensor. Biophys. J . 98: 2327-2336. doi:10.1016/j.bpj.2010.01.046.
Monfregola J, Napolitano G, D'Urso M, Lappalainen P , Ursini MV. Functional characterization of Wiscott Aldrich Syndrome protein and scar homolog (WASH), a bi-modular nucleation promoting factor (NPF) able to interact with biogenesis of lysosome related organelle subunit 2 (BLOS-2) and g-tubulin. J. Biol.Chem. 285: 16951-16957. doi:10.1074/jbc.M109.078501.
Li Q, Song X-W, Zou J, Wang G-K, Kremneva E , Zhu N, Li X-Q, Lappalainen P , Yuan W-J, Qin Y-W, and Jing Q. Attenuation of microRNA-1 de-represses the cytoskeleton regulatory protein twinfilin-1 to provoke cardiac hypertrophy. J. Cell Sci. . 123: 2444-2452. doi:10.1242/jcs.067165.
Rzadzinska AK, Nevalainen EM, Prosser HM, Lappalainen P, Steel KP. MyosinVIIa interacts withTwinfilin-2 at the tips of mechanosensory stereocilia in the inner ear. PLoS One. 4:e7097. doi:10.1371/journal.pone.0007097.
Hotulainen P , Llano O, Smirnov S, Tanhuanpää K, Faix J, Rivera C, Lappalainen P. Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis. J. Cell Biol.185:323-329. doi:10.1083/jcb.200809046.
Skwarek-Maruszewska A, Hotulainen P, Mattila PK , Lappalainen P. Contractility-dependent actin dynamics in cardiomyocyte sarcomeres. J. Cell Sci.122:2119-2126. doi:10.1242/jcs.046805.
Quintero-Monzon O, Jonasson EM, Bertling E, Talarico L, Chaudhry F, Sihvo M, Lappalainen P, Goode BL. The roles of Srv2/CAP oligomerization and binding to cofilin-actin complexes in actin turnover in vivo. J. Biol. Chem. 284:10923-10934. doi:10.1074/jbc.M808760200.
Kardos R, Pozsonyi K, Nevalainen E, Lappalainen P, Nyitrai M, Hild G. The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin. Biophys. J. 96: 2335-43. doi:10.1016/j.bpj.2008.12.3906.
Bach CTT, Creed S, Zhong J, Mahmassani M, Schevzov G, Stehn J, Cowell LN, Naumanen P, Lappalainen P, Gunning PW and O'Neill GM. Tropomyosin isoform expression regulates the transition of adhesions to determine cell speed and direction. Mol. Cell. Biol. 29: 1506-14. doi:10.1128/MCB.00857-08.
Saarikangas J, Zhao H, Pykäläinen A, Laurinmäki P, Mattila PK, Kinnunen P, Butcher SJ, Lappalainen P. Molecular mechanisms of membrane deformation by I-BAR domain proteins. Curr. Biol. 19: 95-107. doi:10.1016/j.cub.2008.12.029.
Nevalainen EM, Skwarek-Maruszewska A, Braun A, Moser M, Lappalainen P. Two biochemically distinct and tissue-specific twinfilin isoforms are generated from mouse twinfilin-2 gene by alternative promoter usage. Biochem. J. 417: 593-600. doi:10.1042/BJ20080608.
Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol.; 182: 51-59. doi:10.1083/jcb.200803100.
Mattila PK, Lappalainen P. Filopodia: molecular architecture and cellular functions. Nat. Rev. Mol. Cell Biol. 9: 446-454. doi:10.1038/nrm2406.
Naumanen P, Lappalainen P, Hotulainen P. Mechanisms of actin stress fibre assembly. J. Microscopy 231: 446-454. doi:10.1111/j.1365-2818.2008.02057.x.
Creed SJ, Bryce N, Naumanen P, Weinberger R, Lappalainen P, Stehn J, Gunning P. Tropomyosin isoforms define distinct microfilament populations with different drug susceptibility. Eur. J Cell Biol. 87: 709-720. doi:10.1016/j.ejcb.2008.03.004.
Chereau D, Boczkowska M, Skwarek-Maruszewska A, Fujiwara I, Hayes DB, Renowski G, Lappalainen P, Pollard TD, Dominguez R. Leiomodin is an actin filament nucleator in muscle cells. Science 320: 239-243. doi:10.1126/science.1155313.
Saarikangas J, Hakanen J, Mattila PK, Grumet M, Salminen M, Lappalainen P. ABBA regulates plasma-membrane and actin dynamics to promote radial glia extension. J. Cell Sci. 121: 1444-1454. doi:10.1242/jcs.027466.
Scita G, Confalonieri S, Lappalainen P, Suetsugu S. IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol. 18: 52-60. doi:10.1016/j.tcb.2007.12.002.
Mattila PK, Pykäläinen A, Saarikangas J, Paavilainen V, Vihinen H, Jokitalo E, Lappalainen P. Missing-In-Metastasis (MIM) and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain like mechanism. J. Cell Biol. 176: 953-964. doi:10.1083/jcb.200609176.
Bertling E, Quintero-Monzon O, Mattila PK, Goode BL, Lappalainen P. Mechanism and biological role of profilin - Srv2/CAP interaction. J. Cell. Sci. 120: 1225-1234. doi:10.1242/jcs.000158.
Paavilainen VO, Hellman M, Helfer E, Koskinen M, Didry D, Annila A, Carlier M-F, Permi P, Lappalainen P. Structural basis and evolutionary origin of actin filament capping by twinfilin. Proc. Natl. Acad. Sci. 104: 3113-3118. doi:10.1073/pnas.0608725104.
Nevalainen E, Paavilainen V, Lappalainen P. Twinfilin family of actin monomer-binding proteins. In P. Lappalainen (Ed.), Actin Monomer Binding Proteins (pp. 53-60). New York, NY: Landes Bioscience. ISBN(Print):9780387464053. ISBN(Electronic):9780387464077. Books at GooglePlay.
Hellman M, Paavilainen VO, Annila A, Lappalainen P, Permi P. NMR assignment of the C-terminal ADF-H domain of an actin monomer binding protein, twinfilin. J. Biomol. NMR, Suppl. 5: 66. doi:10.1007/s10858-006-9052-7.
Hotulainen P, Lappalainen P. Stress-fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173: 383-394. doi:10.1083/jcb.200511093.
Bugyi ;B, Papp G, Hild G, Lőrinczy D, Nevalainen EM, Lappalainen P, Somogyi B, Nyitrai M. Formins regulate actin filament flexibility through long-range allosteric interactions. J. Biol. Chem. 281: 10727-10736. doi:10.1074/jbc.M510252200.
Helfer E, Nevalainen EM, Naumanen P, Romero S, Didry D, Pantaloni D, Lappalainen P, Carlier M-F. Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility. EMBO Journal. 25: 1184–1195. doi:10.1038/sj.emboj.7601019.
Skwarek-Maruszewska A, Hotulainen P, Lappalainen P. Regulation of the actin cytoskeleton by phospholipids. In Advances in Molecular and Cell Biology. Elsevier. Burlington, MA,. vol. 37: 201-219. doi:10.1016/S1569-2558(06)37010-5.
Hotulainen P, Paunola E, Vartiainen MK, Lappalainen P. ADF and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian non-muscle cells. Mol. Biol. Cell 16: 649-664. doi:10.1091/mbc.e04-07-0555.
Hellman M, Paavilainen VO, Annila A, Lappalainen P, Permi P. (1)H, (13)C and (15)N resonance assignments of coactosin, a cytoskeletal regulatory protein. J. Biomol. NMR 30: 365-366. doi:10.1007/s10858-005-1068-x.
Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, Lappalainen P, Goode BL. A high affinity interaction with ADP-G-actin underlies the mechanism and in vivo function of Srv2/cyclase-associated protein (CAP). Mol. Biol. Cell 15: 5158-5171. doi:10.1091/mbc.e04-06-0444.
Hellman M, Paavilainen VO, Naumanen P, Lappalainen P, Annila A, Permi P. Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins. FEBS Letters; 576: 91-96. doi:10.1016/j.febslet.2004.08.068.
Falck S, Paavilainen VO, Wear MA, Grossmann JG, Cooper JA, Lappalainen P. Biological role and structural mechanism of twinfilin – capping protein interaction. EMBO Journal. 23: 3010–3019. doi:10.1038/sj.emboj.7600310.
Bertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, Lappalainen P. Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian non-muscle cells. Mol. Biol. Cell 15: 2312-2323. doi:10.1091/mbc.e04-01-0048.
Paavilainen VO, Bertling E, Falck S, Lappalainen P. Regulation of cytoskeletal dynamics by actin monomer binding proteins. Trends Cell Biol. 14: 386-394. doi:10.1016/j.tcb.2004.05.002.
Hilpelä P., Vartiainen M.K., Lappalainen P. Regulation of the Actin Cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. In: Stenmark H. (eds) Phosphoinositides in Subcellular Targeting and Enzyme Activation, pp 117-163. Current Topics in Microbiology and Immunology, vol 282. Springer, Berlin, Heidelberg. doi:10.1007/978-3-642-18805-3_5.
Vartiainen MK, Sarkkinen EM, Matilainen T, Salminen M, Lappalainen P. Mammals have two twinfilin isoforms whose sub-cellular localizations and tissue distributions are differentially regulated. J. Biol. Chem. 278: 34347-34355. doi:10.1074/jbc.M303642200.
Mattila PK, Salminen M, Yamashiro T, Lappalainen P. Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its carboxyl-terminal WH2 domain. J. Biol. Chem.; 278: 8452-8459. doi:10.1074/jbc.M212113200.
Salmikangas P, van der Ven PFM, Lalowski M, Taivainen A, Zhao F, Suila H, Schröder R, Lappalainen P, Fürst DO, Carpen O. Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly. Hum. Mol. Genetics 12: 189-203. doi:10.1093/hmg/ddg020.
Ojala PJ, Paavilainen VO, Vartiainen MK, Tuma R, Weeds AG, Lappalainen P. The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers. Mol. Biol. Cell 13: 3811-3821. doi:10.1091/mbc.e02-03-0157.
Paavilainen VO, Merckel MC, Falck S, Ojala PJ, Pohl E, Wilmanns M, Lappalainen P. Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolyerizing factor (ADF)/cofilin. J. Biol. Chem. 277: 43089-43095. doi:10.1074/jbc.M208225200.
Band AM, Ali H, Vartiainen MK, Welti S, Lappalainen P, Olkkonen VM, Kuismanen E. Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. FEBS Lett. 531, 513-9. doi:10.1016/S0014-5793(02)03605-0.
Vartiainen MK, Mustonen T, Mattila PK, Ojala PJ, Thesleff I, Partanen J, Lappalainen P. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specificrequirements for actin dynamics. Mol. Biol. Cell 13: 183-194. doi:10.1091/mbc.01-07-0331.
Palmgren S, Vartiainen MK, Lappalainen P. Twinfilin, a molecular mailman for actin monomers. J.Cell Sci. 115: 881-886. Journal of Cell Science.
Paunola E, Mattila PK, Lappalainen P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Letters 513: 92-97. doi:10.1016/S0014-5793(01)03242-2.
Wahlström G, Vartiainen MK, Yamamoto L, Mattila PK, Lappalainen P, Heino TI. Twinfilin is required for actin-dependent developmental processes in Drosophila. J. Cell Biol.; 155: 787-795. doi:10.1083/jcb.200108022.
Palmgren S, Ojala PJ, Wear MA, Cooper JA, Lappalainen P. Interactions with PIP2, ADP-actin monomers and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155: 251-260. doi:10.1083/jcb.200106157.
Ojala PJ, Paavilainen V, Lappalainen P. Identification of yeast cofilin residues specific for actin monomer and PIP2-binding. Biochemistry 40: 15562-15569. doi:10.1021/bi0117697.
Vartiainen M, Ojala PJ, Auvinen P, Peränen J, Lappalainen P. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol. Cell. Biol. 20: 1772-1783. doi:10.1128/MCB.20.5.1772-1783.2000.
Rodal AR, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC. Aip1p interacts with cofilin to disassemble actin filaments. J. Cell Biol. 145: 1251-1264. doi:10.1083/jcb.145.6.1251.
Goode BL, Drubin DG, Lappalainen P. Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142: 723-733. doi:10.1083/jcb.142.3.723.
Lappalainen P, Kessels MM, Cope MJTV, Drubin DG. The ADF homology (ADF-H) domain, a highly exploited actin-binding module. Mol. Biol. Cell 9: 1951-1959. doi:10.1091/mbc.9.8.1951.
Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO Journal 16: 5520-5530. doi:10.1093/emboj/16.18.5520.
Lappalainen P, Drubin DG. Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82. doi:10.1038/40418.
Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC. Structure determination of yeast cofilin. Nature Struct. Biol. 4: 366-369. doi:10.1038/nsb0597-366.