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Cell migration requires the coordinated spatiotemporal regulation of actomyosin contraction and cell protrusion/adhesion. Nonmuscle myosin II (MII) controls Rac1 and Cdc42 activation, and cell protrusion and focal complex formation in migrating cells. However, these mechanisms are poorly understood. Here, we show that MII interacts specifically with multiple Dbl family guanine nucleotide exchange factors (GEFs). Binding is mediated by the conserved tandem Dbl homology-pleckstrin homology module, the catalytic site of these GEFs, with dissociation constants of approximately 0.3 microM. Binding to the GEFs required assembly of the MII into filaments and actin-stimulated ATPase activity. Binding of MII suppressed GEF activity. Accordingly, inhibition of MII ATPase activity caused release of GEFs and activation of Rho GTPases. Depletion of betaPIX GEF in migrating NIH3T3 fibroblasts suppressed lamellipodial protrusions and focal complex formation induced by MII inhibition. The results elucidate a functional link between MII and Rac1/Cdc42 GTPases, which may regulate protrusion/adhesion dynamics in migrating cells.

Titel:	Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: a possible link to Rho family GTPases.
Autor/in / Beteiligte Person:	Lee, CS ; Choi, CK ; Shin, EY ; Schwartz, MA ; Kim, EG
Link:	Full Text Finder (Volltext)
Zeitschrift:	The Journal of cell biology, Jg. 190 (2010-08-23), Heft 4, S. 663-74
Veröffentlichung:	New York : Rockefeller University Press, 2010
Medientyp:	academicJournal
ISSN:	1540-8140 (electronic)
DOI:	10.1083/jcb.201003057
Schlagwort:	Actomyosin metabolism Animals Binding Sites Cell Adhesion Enzyme Activation Guanine Nucleotide Exchange Factors genetics Humans Jurkat Cells Mice Myosin Type II genetics NIH 3T3 Cells Platelet-Derived Growth Factor metabolism Protein Binding RNA, Small Interfering genetics RNA, Small Interfering metabolism Rats Recombinant Fusion Proteins genetics Recombinant Fusion Proteins metabolism Rho Guanine Nucleotide Exchange Factors cdc42 GTP-Binding Protein genetics cdc42 GTP-Binding Protein metabolism rac1 GTP-Binding Protein genetics rac1 GTP-Binding Protein metabolism rho GTP-Binding Proteins genetics Cell Movement physiology Guanine Nucleotide Exchange Factors metabolism Myosin Type II metabolism rho GTP-Binding Proteins metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Language: English [J Cell Biol] 2010 Aug 23; Vol. 190 (4), pp. 663-74. <i>Date of Electronic Publication: </i>2010 Aug 16. MeSH Terms: Cell Movement / physiology ; Guanine Nucleotide Exchange Factors / metabolism ; Myosin Type II / metabolism ; rho GTP-Binding Proteins / metabolism ; Actomyosin / metabolism ; Animals ; Binding Sites ; Cell Adhesion ; Enzyme Activation ; Guanine Nucleotide Exchange Factors / genetics ; Humans ; Jurkat Cells ; Mice ; Myosin Type II / genetics ; NIH 3T3 Cells ; Platelet-Derived Growth Factor / metabolism ; Protein Binding ; RNA, Small Interfering / genetics ; RNA, Small Interfering / metabolism ; Rats ; Recombinant Fusion Proteins / genetics ; Recombinant Fusion Proteins / metabolism ; Rho Guanine Nucleotide Exchange Factors ; cdc42 GTP-Binding Protein / genetics ; cdc42 GTP-Binding Protein / metabolism ; rac1 GTP-Binding Protein / genetics ; rac1 GTP-Binding Protein / metabolism ; rho GTP-Binding Proteins / genetics References: Mol Biol Cell. 2007 Dec;18(12):5081-90. (PMID: 17928407) ; Mol Biol Cell. 2008 May;19(5):2147-53. (PMID: 18287519) ; Nat Cell Biol. 2002 Apr;4(4):294-301. (PMID: 11912491) ; Cell. 1996 Feb 9;84(3):371-9. (PMID: 8608590) ; J Cell Biol. 2004 Feb 2;164(3):427-39. (PMID: 14757754) ; Biochem Soc Trans. 1995 Aug;23(3):456-9. (PMID: 8566347) ; Neuron. 2006 Jan 19;49(2):175-82. (PMID: 16423692) ; J Biol Chem. 2006 Nov 24;281(47):35873-83. (PMID: 17020881) ; J Cell Sci. 2006 Jul 1;119(Pt 13):2654-66. (PMID: 16787945) ; J Cell Biol. 2000 Aug 7;150(3):627-42. (PMID: 10931873) ; Mol Biol Cell. 2006 Oct;17(10):4435-45. (PMID: 16855019) ; J Neurobiol. 2006 Jul;66(8):847-67. (PMID: 16673385) ; J Biol Chem. 1991 Dec 15;266(35):23936-44. (PMID: 1748666) ; Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16189-94. (PMID: 18838676) ; Genes Cells. 1998 Mar;3(3):177-88. (PMID: 9619630) ; J Biol Chem. 2005 Jun 17;280(24):22769-75. (PMID: 15845534) ; Science. 2003 Mar 14;299(5613):1743-7. (PMID: 12637748) ; Am J Physiol. 1999 Jun;276(6):C1312-24. (PMID: 10362594) ; J Cell Biol. 2000 Oct 16;151(2):249-62. (PMID: 11038173) ; J Physiol. 2000 Jan 15;522 Pt 2:177-85. (PMID: 10639096) ; Mol Cell. 1998 Jan;1(2):183-92. (PMID: 9659915) ; Genes Dev. 2002 Jul 1;16(13):1587-609. (PMID: 12101119) ; J Cell Sci. 2005 Jun 15;118(Pt 12):2579-87. (PMID: 15928049) ; J Biol Chem. 2004 Aug 20;279(34):35557-63. (PMID: 15205456) ; Am J Physiol. 1991 Dec;261(6 Pt 2):F1038-45. (PMID: 1721494) ; J Cell Sci. 1998 Aug;111 ( Pt 15):2085-95. (PMID: 9664030) ; J Cell Sci. 2008 Jan 1;121(Pt 1):11-8. (PMID: 18096687) ; J Biol Chem. 2002 Nov 29;277(48):46512-7. (PMID: 12237319) ; J Cell Biol. 2007 Feb 26;176(5):573-80. (PMID: 17312025) ; Nature. 1975 Aug 14;256(5518):597-8. (PMID: 170529) ; Cell. 1996 Feb 9;84(3):359-69. (PMID: 8608589) ; Cell. 2006 Jun 30;125(7):1361-74. (PMID: 16814721) ; J Biol Chem. 2004 Jan 16;279(3):1994-2004. (PMID: 14557270) ; Nat Cell Biol. 2007 Mar;9(3):299-309. (PMID: 17310241) ; J Biol Chem. 1999 May 7;274(19):13198-204. (PMID: 10224076) ; EMBO J. 1999 Feb 1;18(3):578-85. (PMID: 9927417) ; J Cell Biol. 1999 Nov 29;147(5):1009-22. (PMID: 10579721) ; Mol Biol Cell. 2008 Dec;19(12):5156-67. (PMID: 18843042) ; J Cell Biol. 2002 Jul 8;158(1):153-64. (PMID: 12105187) ; J Cell Biol. 1985 Apr;100(4):1031-40. (PMID: 3920222) ; Cell Cycle. 2006 Jun;5(11):1234-9. (PMID: 16721066) ; Nat Cell Biol. 2008 Sep;10(9):1039-50. (PMID: 19160484) Grant Information: R01 GM047214 United States GM NIGMS NIH HHS; R01 GM47214 United States GM NIGMS NIH HHS Substance Nomenclature: 0 (Arhgef7 protein, mouse) ; 0 (Guanine Nucleotide Exchange Factors) ; 0 (Platelet-Derived Growth Factor) ; 0 (RNA, Small Interfering) ; 0 (Recombinant Fusion Proteins) ; 0 (Rho Guanine Nucleotide Exchange Factors) ; 9013-26-7 (Actomyosin) ; EC 3.6.1.- (Myosin Type II) ; EC 3.6.5.2 (cdc42 GTP-Binding Protein) ; EC 3.6.5.2 (rac1 GTP-Binding Protein) ; EC 3.6.5.2 (rho GTP-Binding Proteins) Entry Date(s): Date Created: 20100818 Date Completed: 20100927 Latest Revision: 20211020 Update Code: 20240513 PubMed Central ID: PMC2928003

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Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: a possible link to Rho family GTPases.