Publications v2

Publication list of Lappalainen Lab

2018

Jiu Y, Kumari R, Fenix AM, Schaible N, Liu X, Varjosalo M, Krishnan R, Burnette DT, Lappalainen P (2018): Myosin-18B promotes the assembly of myosin II stacks for maturation of contractile actomyosin bundles. Curr. Biol. (in press).

Ciuba K, Hawkes W, Tojkander S, Kogan K, Engel U, Iskratsch T, Lappalainen P (2018): Calponin-3 is critical for coordinated contractility of actin stress fibers. Sci. Reports. Dec 5;8(1):17670.

Tsai FC, Bertin A, Bousquet H, Manzi J, Senju Y, Picas L, Miserey-Lenkei S, Lappalainen P, Lemichez E, Coudrier E, Bassereau P (2018): Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner. eLife 7: e37262.

Senju Y, Lappalainen P (2018): Regulation of actin dynamics by PI(4,5)P2 in cell migration and endocytosis. (2018) Curr. Opin. Cell Biol. Sep 4;56:7-13.

Tojkander S, Ciuba K, Lappalainen P (2018): CaMKK2 regulates mechanosensitive assembly of contractile actin stress fibers. Cell Reports 24: 11-19.

*Kotila T, *Kogan K, Enkavi G, Guo S, Vattulainen I, Goode BL, Lappalainen P (2018): Structural basis of actin monomer re-charging by cyclase-associated protein. Nature Commun. 9:1892. *equal contribution.

Hakala M, Kalimeri M, Enkavi G, Vattulainen I, Lappalainen P (2018): Molecular mechanism for inhibition of twinfilin by phosphoinositides. J Biol. Chem. 293: 4818-4829.

2017

Senju Y, Kalimeri M, Koskela EV, Somerharju P, Zhao H, Vattulainen I, Lappalainen P (2017): Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides. Proc. Natl. Acad. Sci. 114: E8977-E8986.

Lehtimäki JI, Fenix AM, Kotila T, Balistreri G, Paavolainen L, Varjosalo M, Burnette BT, Lappalainen P (2017): UNC-45a promotes myosin folding and stress fiber assembly. J Cell Biol. ( 216: 4053-4072.

Stritt S, Beck S, Becker IC, Vogtle T, Hakala M, Heinze KG, Du X, Bender M, Braun A, Lappalainen P, Nieswandt B (2017): Twinfilin 2a is a regulator of platelet reactivity and turnover in mice. Blood. 130: 1746-1756.

Khan MH, Salomaa SI, Jacquemet G, Butt U, Miihkinen M, Deguchi T, Kremneva E, Lappalainen P, Humphries MJ, Pouwels J (2017): The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex. J Cell Sci. 130: 3094-3107.

Wioland H, Guichard B, Senju Y, Myram S, Lappalainen P, Jegou A, Romet-Lemonne G (2017): ADF/cofilin accelerates actin dynamics by severing filaments and promoting their depolymerization at both ends. Curr. Biol. 27: 1956-1967.

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 (2017): Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation. Nat. Commun. 8:15839.

Gateva G, Kremneva E, Reindl T, Kotila T, Kogan K, Gressin L, Gunning PW, Manstein DJ, Michelot A, Lappalainen P (2017): Tropomyosin isoforms specify functionally distinct actin filament populations in vitro. Curr. Biol. 27, 705-713.

Pfisterer S, Gateva G, Horvath P, Pirhonen J, Salo V, Karhinen L, Varjosalo M, Ryhänen S, Lappalainen P, Ikonen E (2017): Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage. Nature Commun. 8:14858.

Jiu Y, Peränen J, Schaible N, Cheng F, Eriksson JE, Krishnan R, Lappalainen P (2017): Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA. J Cell Sci. 130: 892-902.

Lehtimäki J, Hakala M, Lappalainen P (2017): Actin Filament Structures in Migrating Cells. Handb Exp Pharmacology235:123-152.

2016

Lappalainen P (2016): Actin-binding proteins: the long road to understanding the dynamic landscape of cellular actin networks. Mol Biol Cell.,27:2519-2522.

 

2015

Tojkander S, Gateva G, Husain A, Krishnan R, Lappalainen P (2015): Generation of contractile actomyosin bundles depends on mechanosensitive actin filament assembly and disassembly. eLife, 4:e06126.

Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R (2015): How leiomodin and tropomodulin use a common fold for different actin assembly functions. Nat. Commun. 15;6:8314.

Prévost C, Zhao H, Manzi J, Lemichez E, Lappalainen P, Callan-Jones A,  Bassereau P (2015): IRSp53 senses negative membrane curvature and phase separates along membrane tubules. Nat. Commun. 15:6:8529.

Gunning PW, Hardeman EC, Lappalainen P, Mulvihill DP (2015):  Tropomyosin: Master regulator of actin filament function in the cytoskeleton. J. Cell Sci. 128: 2965-74.

Jiu Y, Lehtimäki J, Tojkander S, Cheng F, Jäälinoja H, Liu X, Varjosalo M, Eriksson JE, Lappalainen P (2015). Bidirectional interplay between vimentin intermediate filaments and contractile actin stress fibers. Cell Reports 11: 1511-1518.

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 (2015): MIM-induced membrane bending promotes dendritic spine initiation. Dev. Cell 33: 644-659.

2000

Vartiainen M, Ojala PJ, Auvinen P, Peränen J, Lappalainen P (2000): Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol. Cell. Biol. 20: 1772-1783.

1997-1999 (at UC Berkeley)

Rodal AR, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC (1999): Aip1p interacts with cofilin to disassemble actin filaments. J. Cell Biol. 145: 1251-1264.

Goode BL, Drubin DG, Lappalainen P (1998): Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142: 723-733.

Lappalainen P, Kessels MM, Cope MJTV, Drubin DG (1998): The ADF homology (ADF-H) domain, a highly exploited actin-binding module. Mol. Biol. Cell 9: 1951-1959.

Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG (1997): Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO Journal 16: 5520-5530.

Lappalainen P, Drubin DG (1997): Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82.

Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC (1997): Structure determination of yeast cofilin. Nature Struct. Biol. 4: 366-369.