The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin

Walders-Harbeck B, Khaitlina SY, Hinssen H, Jockusch BM, Illenberger S (2002)
FEBS LETTERS 529(2-3): 275-280.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Walders-Harbeck, B; Khaitlina, SY; Hinssen, HorstUniBi; Jockusch, BM; Illenberger, S
Abstract / Bemerkung
The vasodilator-stimulated phosphoprotein (VASP) functions as a cellular regulator of actin dynamics. VASP may initialise actin polymerisation, suggesting a direct interaction with monomeric actin. The present study demonstrates that VASP directly binds to actin monomers and that complex formation depends on a conserved four amino acid motif in the EVH2 domain. Point mutations within this motif drastically weaken VASP/G-actin interactions, thereby abolishing any actin-nucleating activity of VASP. Additionally, actin nucleation was found to depend on VASP oligomerisation since VASP monomers fail to induce the formation of actin filaments. Phosphorylation negatively affects VASP/G-actin interactions preventing VASP-induced actin filament formation. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Stichworte
Ena/Mena/vasodilator-stimulated phosphoprotein; actin dynamics; G-actin; nucleation; polymerisation
Erscheinungsjahr
2002
Zeitschriftentitel
FEBS LETTERS
Band
529
Ausgabe
2-3
Seite(n)
275-280
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1613442

Zitieren

Walders-Harbeck B, Khaitlina SY, Hinssen H, Jockusch BM, Illenberger S. The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS LETTERS. 2002;529(2-3):275-280.
Walders-Harbeck, B., Khaitlina, S. Y., Hinssen, H., Jockusch, B. M., & Illenberger, S. (2002). The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS LETTERS, 529(2-3), 275-280. https://doi.org/10.1016/S0014-5793(02)03356-2
Walders-Harbeck, B, Khaitlina, SY, Hinssen, Horst, Jockusch, BM, and Illenberger, S. 2002. “The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin”. FEBS LETTERS 529 (2-3): 275-280.
Walders-Harbeck, B., Khaitlina, S. Y., Hinssen, H., Jockusch, B. M., and Illenberger, S. (2002). The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS LETTERS 529, 275-280.
Walders-Harbeck, B., et al., 2002. The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS LETTERS, 529(2-3), p 275-280.
B. Walders-Harbeck, et al., “The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin”, FEBS LETTERS, vol. 529, 2002, pp. 275-280.
Walders-Harbeck, B., Khaitlina, S.Y., Hinssen, H., Jockusch, B.M., Illenberger, S.: The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS LETTERS. 529, 275-280 (2002).
Walders-Harbeck, B, Khaitlina, SY, Hinssen, Horst, Jockusch, BM, and Illenberger, S. “The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin”. FEBS LETTERS 529.2-3 (2002): 275-280.

55 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Computational and experimental analysis of bioactive peptide linear motifs in the integrin adhesome.
O'Brien KT, Golla K, Kranjc T, O'Donovan D, Allen S, Maguire P, Simpson JC, O'Connell D, Moran N, Shields DC., PLoS One 14(1), 2019
PMID: 30689642
The polarity protein Angiomotin p130 controls dendritic spine maturation.
Wigerius M, Quinn D, Diab A, Clattenburg L, Kolar A, Qi J, Krueger SR, Fawcett JP., J Cell Biol 217(2), 2018
PMID: 29317530
Translocated in liposarcoma regulates the distribution and function of mammalian enabled, a modulator of actin dynamics.
Sugiura T, Matsuda S, Kurosaka S, Nakai N, Fukumoto K, Takahashi T, Maruyama H, Imaizumi K, Matsumoto M, Takumi T., FEBS J 283(8), 2016
PMID: 26896672
Vasodilator-Stimulated Phosphoprotein Activity Is Required for Coxiella burnetii Growth in Human Macrophages.
Colonne PM, Winchell CG, Graham JG, Onyilagha FI, MacDonald LJ, Doeppler HR, Storz P, Kurten RC, Beare PA, Heinzen RA, Voth DE., PLoS Pathog 12(10), 2016
PMID: 27711191
WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.
Havrylenko S, Noguera P, Abou-Ghali M, Manzi J, Faqir F, Lamora A, Guérin C, Blanchoin L, Plastino J., Mol Biol Cell 26(1), 2015
PMID: 25355952
VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module.
Oldenburg J, van der Krogt G, Twiss F, Bongaarts A, Habani Y, Slotman JA, Houtsmuller A, Huveneers S, de Rooij J., Sci Rep 5(), 2015
PMID: 26611125
VASP activation via the Gα13/RhoA/PKA pathway mediates cucurbitacin-B-induced actin aggregation and cofilin-actin rod formation.
Zhang YT, Xu LH, Lu Q, Liu KP, Liu PY, Ji F, Liu XM, Ouyang DY, He XH., PLoS One 9(4), 2014
PMID: 24691407
Capping protein regulators fine-tune actin assembly dynamics.
Edwards M, Zwolak A, Schafer DA, Sept D, Dominguez R, Cooper JA., Nat Rev Mol Cell Biol 15(10), 2014
PMID: 25207437
Differential roles of cAMP and cGMP in megakaryocyte maturation and platelet biogenesis.
Begonja AJ, Gambaryan S, Schulze H, Patel-Hett S, Italiano JE, Hartwig JH, Walter U., Exp Hematol 41(1), 2013
PMID: 22981933
Multiple actin binding domains of Ena/VASP proteins determine actin network stiffening.
Gentry BS, van der Meulen S, Noguera P, Alonso-Latorre B, Plastino J, Koenderink GH., Eur Biophys J 41(11), 2012
PMID: 23052975
Heat shock protein DnaK--substrate of actin-specific bacterial protease ECP32.
Morozova AV, Khaitlina SY, Malinin AY., Biochemistry (Mosc) 76(4), 2011
PMID: 21585321
VASP phosphorylation at serine239 regulates the effects of NO on smooth muscle cell invasion and contraction of collagen.
Defawe OD, Kim S, Chen L, Huang D, Kenagy RD, Renné T, Walter U, Daum G, Clowes AW., J Cell Physiol 222(1), 2010
PMID: 19798690
[The cytoskeletal protein zyxin--a universal regulator of cell adhesion and gene expression]
Ermolina LV, Martynova NIu, Zaraĭskiĭ AG., Bioorg Khim 36(1), 2010
PMID: 20386576
Characterization of a novel interaction between vasodilator-stimulated phosphoprotein and Abelson interactor 1 in human platelets: a concerted computational and experimental approach.
Dittrich M, Strassberger V, Fackler M, Tas P, Lewandrowski U, Sickmann A, Walter U, Dandekar T, Birschmann I., Arterioscler Thromb Vasc Biol 30(4), 2010
PMID: 20110575
Critical role of serum response factor in pulmonary myofibroblast differentiation induced by TGF-beta.
Sandbo N, Kregel S, Taurin S, Bhorade S, Dulin NO., Am J Respir Cell Mol Biol 41(3), 2009
PMID: 19151320
Probing for actinase activity of protealysin.
Tsaplina OA, Efremova TN, Kever LV, Komissarchik YY, Demidyuk IV, Kostrov SV, Khaitlina SY., Biochemistry (Mosc) 74(6), 2009
PMID: 19645670
Biochemical analysis of the human EVL domains in homologous recombination.
Takaku M, Machida S, Nakayama S, Takahashi D, Kurumizaka H., FEBS J 276(20), 2009
PMID: 19725871
Grimelysin, a novel metalloprotease from Serratia grimesii, is similar to ECP32.
Bozhokina E, Khaitlina S, Adam T., Biochem Biophys Res Commun 367(4), 2008
PMID: 18190782
Ena/VASP: proteins at the tip of the nervous system.
Drees F, Gertler FB., Curr Opin Neurobiol 18(1), 2008
PMID: 18508258
Role of vasodilator-stimulated phosphoprotein in cGMP-mediated protection of human pulmonary artery endothelial barrier function.
Rentsendorj O, Mirzapoiazova T, Adyshev D, Servinsky LE, Renné T, Verin AD, Pearse DB., Am J Physiol Lung Cell Mol Physiol 294(4), 2008
PMID: 18281604
Ena/VASP proteins capture actin filament barbed ends.
Pasic L, Kotova T, Schafer DA., J Biol Chem 283(15), 2008
PMID: 18283104
Dynamic length regulation of sensory stereocilia.
Manor U, Kachar B., Semin Cell Dev Biol 19(6), 2008
PMID: 18692583
VASP governs actin dynamics by modulating filament anchoring.
Trichet L, Campàs O, Sykes C, Plastino J., Biophys J 92(3), 2007
PMID: 17098798
Ena/VASP proteins have an anti-capping independent function in filopodia formation.
Applewhite DA, Barzik M, Kojima S, Svitkina TM, Gertler FB, Borisy GG., Mol Biol Cell 18(7), 2007
PMID: 17475772
Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation.
Dwivedy A, Gertler FB, Miller J, Holt CE, Lebrand C., Development 134(11), 2007
PMID: 17507414
Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility.
Holtzman JH, Woronowicz K, Golemi-Kotra D, Schepartz A., Biochemistry 46(47), 2007
PMID: 17973491
Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.
Boëda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M., Mol Cell 28(6), 2007
PMID: 18158903
VASP-dependent regulation of actin cytoskeleton rigidity, cell adhesion, and detachment.
Galler AB, García Arguinzonis MI, Baumgartner W, Kuhn M, Smolenski A, Simm A, Reinhard M., Histochem Cell Biol 125(5), 2006
PMID: 16267652
Understanding the role of the G-actin-binding domain of Ena/VASP in actin assembly.
Chereau D, Dominguez R., J Struct Biol 155(2), 2006
PMID: 16684607
RNAi knockdown of the focal adhesion protein TES reveals its role in actin stress fibre organisation.
Griffith E, Coutts AS, Black DM., Cell Motil Cytoskeleton 60(3), 2005
PMID: 15662727
Cloning and developmental expression of Xenopus Enabled (Xena).
Xanthos JB, Wanner SJ, Miller JR., Dev Dyn 233(2), 2005
PMID: 15778995
Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins.
Barzik M, Kotova TI, Higgs HN, Hazelwood L, Hanein D, Gertler FB, Schafer DA., J Biol Chem 280(31), 2005
PMID: 15939738
Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C.
Chitaley K, Chen L, Galler A, Walter U, Daum G, Clowes AW., FEBS Lett 556(1-3), 2004
PMID: 14706852
TetraThymosinbeta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats.
Van Troys M, Ono K, Dewitte D, Jonckheere V, De Ruyck N, Vandekerckhove J, Ono S, Ampe C., Mol Biol Cell 15(10), 2004
PMID: 15269284
The actin cytoskeleton in normal and pathological cell motility.
Lambrechts A, Van Troys M, Ampe C., Int J Biochem Cell Biol 36(10), 2004
PMID: 15203104
The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
Kühnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV., Proc Natl Acad Sci U S A 101(49), 2004
PMID: 15569942
Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration.
Krause M, Dent EW, Bear JE, Loureiro JJ, Gertler FB., Annu Rev Cell Dev Biol 19(), 2003
PMID: 14570581
Do filopodia enable the growth cone to find its way?
Koleske AJ., Sci STKE 2003(183), 2003
PMID: 12759482
A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity.
Grosse R, Copeland JW, Newsome TP, Way M, Treisman R., EMBO J 22(12), 2003
PMID: 12805219
Function and regulation of Ena/VASP proteins.
Kwiatkowski AV, Gertler FB, Loureiro JJ., Trends Cell Biol 13(7), 2003
PMID: 12837609
Do inflammatory mediators influence the contribution of airway smooth muscle contraction to airway hyperresponsiveness in asthma?
Fernandes DJ, Mitchell RW, Lakser O, Dowell M, Stewart AG, Solway J., J Appl Physiol (1985) 95(2), 2003
PMID: 12851423
How VASP enhances actin-based motility.
Samarin S, Romero S, Kocks C, Didry D, Pantaloni D, Carlier MF., J Cell Biol 163(1), 2003
PMID: 14557252

31 References

Daten bereitgestellt von Europe PubMed Central.

The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts.
Reinhard M, Halbrugge M, Scheer U, Wiegand C, Jockusch BM, Walter U., EMBO J. 11(6), 1992
PMID: 1318192
The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate.
Huttelmaier S, Mayboroda O, Harbeck B, Jarchau T, Jockusch BM, Rudiger M., Curr. Biol. 8(9), 1998
PMID: 9560340
VASP dynamics during lamellipodia protrusion.
Rottner K, Behrendt B, Small JV, Wehland J., Nat. Cell Biol. 1(5), 1999
PMID: 10559946
Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility.
Bear JE, Svitkina TM, Krause M, Schafer DA, Loureiro JJ, Strasser GA, Maly IV, Chaga OY, Cooper JA, Borisy GG, Gertler FB., Cell 109(4), 2002
PMID: 12086607
Mena is required for neurulation and commissure formation.
Lanier LM, Gates MA, Witke W, Menzies AS, Wehman AM, Macklis JD, Kwiatkowski D, Soriano P, Gertler FB., Neuron 22(2), 1999
PMID: 10069337
Directed actin polymerization is the driving force for epithelial cell-cell adhesion.
Vasioukhin V, Bauer C, Yin M, Fuchs E., Cell 100(2), 2000
PMID: 10660044
VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs.
Reinhard M, Rudiger M, Jockusch BM, Walter U., FEBS Lett. 399(1-2), 1996
PMID: 8980130
The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin.
Brindle NP, Holt MR, Davies JE, Price CJ, Critchley DR., Biochem. J. 318 ( Pt 3)(), 1996
PMID: 8836115
Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins.
Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM., J. Biol. Chem. 275(29), 2000
PMID: 10801818
Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP.
Huttelmaier S, Harbeck B, Steffens O, Messerschmidt T, Illenberger S, Jockusch BM., FEBS Lett. 451(1), 1999
PMID: 10356985
The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins.
Reinhard M, Giehl K, Abel K, Haffner C, Jarchau T, Hoppe V, Jockusch BM, Walter U., EMBO J. 14(8), 1995
PMID: 7737110
Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin.
Harbeck B, Huttelmaier S, Schluter K, Jockusch BM, Illenberger S., J. Biol. Chem. 275(40), 2000
PMID: 10882740
Cell motility: proline-rich proteins promote protrusions.
Holt MR, Koffer A., Trends Cell Biol. 11(1), 2001
PMID: 11146297
ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity.
Fradelizi J, Noireaux V, Plastino J, Menichi B, Louvard D, Sykes C, Golsteyn RM, Friederich E., Nat. Cell Biol. 3(8), 2001
PMID: 11483954
Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility.
Skoble J, Auerbuch V, Goley ED, Welch MD, Portnoy DA., J. Cell Biol. 155(1), 2001
PMID: 11581288
Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I.
Schluter K, Schleicher M, Jockusch BM., J. Cell. Sci. 111 ( Pt 22)(), 1998
PMID: 9788869
The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament.
Khaitlina SY, Moraczewska J, Strzelecka-Golaszewska H., Eur. J. Biochem. 218(3), 1993
PMID: 8281943
Purification and characterization of the proteinase ECP 32 from Escherichia coli A2 strain.
Matveyev VV, Usmanova AM, Morozova AV, Collins JH, Khaitlina SY., Biochim. Biophys. Acta 1296(1), 1996
PMID: 8765229
The actin binding site of thymosin beta 4 mapped by mutational analysis.
Van Troys M, Dewitte D, Goethals M, Carlier MF, Vandekerckhove J, Ampe C., EMBO J. 15(2), 1996
PMID: 8617195
Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain.
Khaitlina SYu , Collins JH, Kuznetsova IM, Pershina VP, Synakevich IG, Turoverov KK, Usmanova AM., FEBS Lett. 279(1), 1991
PMID: 1995340
Signaling to actin dynamics.
Machesky LM, Insall RH., J. Cell Biol. 146(2), 1999
PMID: 10427083
Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast.
Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A., Nat. Cell Biol. 4(1), 2002
PMID: 11740490
Yeast formins regulate cell polarity by controlling the assembly of actin cables.
Sagot I, Klee SK, Pellman D., Nat. Cell Biol. 4(1), 2002
PMID: 11740491
Conformational changes in actin induced by its interaction with gelsolin.
Khaitlina S, Hinssen H., Biophys. J. 73(2), 1997
PMID: 9251809
Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody.
Gonsior SM, Platz S, Buchmeier S, Scheer U, Jockusch BM, Hinssen H., J. Cell. Sci. 112 ( Pt 6)(), 1999
PMID: 10036230
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 12372613
PubMed | Europe PMC

Suchen in

Google Scholar