Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration.
about
IQGAP1 promotes neurite outgrowth in a phosphorylation-dependent mannerClustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteinsAlterations in vasodilator-stimulated phosphoprotein (VASP) phosphorylation: associations with asthmatic phenotype, airway inflammation and beta2-agonist use.Human Mena associates with Rac1 small GTPase in glioblastoma cell linesAbl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinaseMechanism of filopodia initiation by reorganization of a dendritic network.Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146.WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.Vasodilator-stimulated phosphoprotein (VASP) induces actin assembly in dendritic spines to promote their development and potentiate synaptic strength.Ena/VASP proteins have an anti-capping independent function in filopodia formation.Spatial regulation of the cAMP-dependent protein kinase during chemotactic cell migrationEna/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts.A WAVE-1 and WRP signaling complex regulates spine density, synaptic plasticity, and memory.The actin regulators Enabled and Diaphanous direct distinct protrusive behaviors in different tissues during Drosophila development.5'-Inositol phosphatase SHIP2 recruits Mena to stabilize invadopodia for cancer cell invasion.The alternatively-included 11a sequence modifies the effects of Mena on actin cytoskeletal organization and cell behaviorBlood vessel endothelium-directed tumor cell streaming in breast tumors requires the HGF/C-Met signaling pathway.Functional roles of VASP phosphorylation in the regulation of chemotaxis and osmotic stress responseContribution of Ena/VASP proteins to intracellular motility of listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerizationEna/VASP regulates mDia2-initiated filopodial length, dynamics, and function.Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteinsVasodilator-stimulated phosphoprotein regulates proliferation and growth inhibition by nitric oxide in vascular smooth muscle cells.VASP is a processive actin polymerase that requires monomeric actin for barbed end association.VASP phosphorylation at serine239 regulates the effects of NO on smooth muscle cell invasion and contraction of collagenIdentification of invasion specific splice variants of the cytoskeletal protein Mena present in mammary tumor cells during invasion in vivo.The cell biology of Listeria monocytogenes infection: the intersection of bacterial pathogenesis and cell-mediated immunity.Mammalian enabled (Mena) is a critical regulator of cardiac function.Mena invasive (MenaINV) promotes multicellular streaming motility and transendothelial migration in a mouse model of breast cancerDo filopodia enable the growth cone to find its way?Molecular cloning of hMena (ENAH) and its splice variant hMena+11a: epidermal growth factor increases their expression and stimulates hMena+11a phosphorylation in breast cancer cell lines.Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.Syndecan-2 induces filopodia and dendritic spine formation via the neurofibromin-PKA-Ena/VASP pathway.Mena invasive (Mena(INV)) and Mena11a isoforms play distinct roles in breast cancer cell cohesion and association with TMEMHow VASP enhances actin-based motilityMena-GRASP65 interaction couples actin polymerization to Golgi ribbon linkingMena binds α5 integrin directly and modulates α5β1 function.Selectivity in subunit composition of Ena/VASP tetramers.Expression and Distribution Characteristics of Human Ortholog of Mammalian Enabled (hMena) in GliomaVasodilator-stimulated phosphoprotein restricts cell-to-cell spread of Shigella flexneri at the cell periphery
P2860
Q24294255-705070BA-B56F-42B6-BC29-A3A9296331E7Q24655828-30F8438D-E7A8-403C-9726-63820D5B5E14Q24678535-238CC849-4609-46A3-AFE3-F409E60D316CQ25257666-A0C99F50-249E-45A8-814A-83E15D29AC2FQ27350493-ED37FE71-E03A-43FE-8E28-7525E02C4385Q28188375-96C75C2B-840B-4282-BE01-87A0DF3B2EEEQ29616648-C51AC2D7-BA07-4E6B-B526-AF6FE46ECA4FQ30164911-595C2403-3915-4766-861A-3BF5EA823C96Q30407475-2E29C20C-063B-4BCC-8AA3-CAD78731BF53Q30429783-AC34D29E-1B00-4283-B4E7-994BB0D9F5D6Q30444426-C65CEFE8-8059-437A-9FAB-2D0E0AC48CC1Q30476244-C51CFA8A-72F6-4AE4-B14D-4CAC6A875585Q30476860-AA3B0967-F4D5-4392-9F4C-27D7E8313694Q30542623-97C6047B-E354-408F-A908-04ABF2A15CA7Q30592242-875ACEE0-7B37-4D6C-BA3B-11BD44CCBB35Q30810808-BF082451-7535-4B1D-B703-978A0A30CF2DQ30823188-8349B9C2-C184-4664-A7E4-3022A4B682E0Q33665092-E2DEF5E9-1580-4499-9996-8A1C14E2A3CAQ33787522-9CB1F667-F64D-43D4-B5B3-2B828BDA4AD3Q33893682-3E5205A7-1B31-496D-B7EB-15F9156DDAD7Q34104692-7060D829-2261-4400-BB09-FB20493BC927Q34345554-88C18448-5DC9-4CCA-B93F-537EE64C986CQ34406700-92470EBB-9495-47FB-A59A-19BBE0F74EDFQ34412426-EBDC0263-304C-4D02-BA3F-5092654B2970Q34567261-B2E4B245-B29C-4303-B0A5-B2762C00517AQ34592450-999DEC43-6601-4315-9831-6A257E43B8B9Q34774585-7E362433-0906-40DB-B75C-55DC8C4301DFQ34979743-84300460-E4DB-48BF-8217-5889324652CAQ35041274-3E3299A3-757E-41AC-B25A-C65BDCCFDC24Q35132220-49E7D546-5DCA-41CF-BCAD-3E6D3C83101BQ35165997-732CF4FB-FBF1-430F-B7E1-71747994D68BQ35979105-254E28B2-5A75-4DD0-AB5C-328FBA9B95B8Q36118445-B27D77C0-EF08-4746-8BA1-2F8D6319DB5BQ36283722-275626BE-9482-4FF5-8077-969F92346CA0Q36324377-71495EFB-224C-459E-BC71-2E2C2C7827CAQ36412954-9C3EA5D1-2AEE-48AD-A79B-F94AC3E20879Q36444281-FB3B48D1-8801-4A5E-9798-9AF8A170431DQ36487016-5F88E096-8B92-4481-8B92-B3B1610BB8A0Q36551102-C965711A-8177-4D1C-AC17-D7AC57B5C858Q36725569-475ADC50-A631-4E0B-B83F-E73F021FC22B
P2860
Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Critical roles of phosphorylat ...... unction during cell migration.
@ast
Critical roles of phosphorylat ...... unction during cell migration.
@en
type
label
Critical roles of phosphorylat ...... unction during cell migration.
@ast
Critical roles of phosphorylat ...... unction during cell migration.
@en
prefLabel
Critical roles of phosphorylat ...... unction during cell migration.
@ast
Critical roles of phosphorylat ...... unction during cell migration.
@en
P2093
P2860
P356
P1476
Critical roles of phosphorylat ...... unction during cell migration.
@en
P2093
Adam V Kwiatkowski
Douglas A Rubinson
Frank B Gertler
Gretchen A Baltus
James E Bear
Joseph J Loureiro
P2860
P304
P356
10.1091/MBC.E01-10-0102
P577
2002-07-01T00:00:00Z