The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate.
about
Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase IRecruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesionStructural basis for amplifying vinculin activation by talinRegulation of Bin1 SH3 domain binding by phosphoinositidesActin dynamics in plateletsDual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinityJanus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transductionRaver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteinsRole of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenesCharacterization of palladin, a novel protein localized to stress fibers and cell adhesions.Vinculin and metavinculin: oligomerization and interactions with F-actinVASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin moduleThe F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alphaSpatial distribution and functional significance of activated vinculin in living cellsVinculin controls focal adhesion formation by direct interactions with talin and actin.A lipid-regulated docking site on vinculin for protein kinase C.Talin contains three similar vinculin-binding sites predicted to form an amphipathic helixReversible tumorigenesis induced by deficiency of vasodilator-stimulated phosphoprotein.Monomeric and dimeric conformation of the vinculin tail five-helix bundle in solution studied by EPR spectroscopy.Focal adhesion assembly in myofibroblasts fosters a microenvironment that promotes tumor growthComparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites.Lipid binding promotes oligomerization and focal adhesion activity of vinculinHeterozygous inactivation of the vinculin gene predisposes to stress-induced cardiomyopathyVasodilator-stimulated phosphoprotein (VASP) regulates actin polymerization and contraction in airway smooth muscle by a vinculin-dependent mechanism.New insights into vinculin function and regulation.GxcDD, a putative RacGEF, is involved in Dictyostelium developmentαE-catenin is an autoinhibited molecule that coactivates vinculin.Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution.Vinculin Interacts with the Chlamydia Effector TarP Via a Tripartite Vinculin Binding Domain to Mediate Actin Recruitment and Assembly at the Plasma MembraneDifferential lipid binding of vinculin isoforms promotes quasi-equivalent dimerizationTumor suppressor activity of profilin requires a functional actin binding site.Diversity of polyproline recognition by EVH1 domains.The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics.p38 mitogen-activated protein kinase interacts with vinculin at focal adhesions during fatty acid-stimulated cell adhesion.Vinculin, an adapter protein in control of cell adhesion signalling.Mechanisms and Functions of Vinculin Interactions with Phospholipids at Cell Adhesion Sites.Neutrophil beta2 integrin inhibition by enhanced interactions of vasodilator-stimulated phosphoprotein with S-nitrosylated actin.Cell-matrix adhesions differentially regulate fascin phosphorylation.Role of vinculin in cellular mechanotransduction.
P2860
Q22254250-55AE0C61-899A-4726-9FCF-2CC5D03ED232Q24324823-C45DD7C1-5F2A-4235-A2A9-B0CBB8D458D4Q24336004-621C6F3D-A9E7-42F3-B8C7-8A56EE934969Q24561373-1E184B9A-5FDD-4840-A1C6-7257885C0E05Q24603193-88771439-0FD2-48D0-8182-C7675B14D4F4Q24630138-A87D7CD8-B53A-4BD6-A891-0E2BEFAAA2ACQ24654170-356054F4-806B-4021-B226-B5E89762F463Q24685280-0F2CB6E4-7D08-400E-860E-796B30172DD7Q24685793-C6694664-4B6A-4CB1-A7B4-FDDB198C79F9Q24685916-AFAF3083-7262-4C09-9BC4-1DE6D6C3DD51Q27009352-15B757E5-18B6-40C2-9592-3B56EEBEFE79Q27304987-A9241267-170D-4D51-AB28-9FFC168A023CQ28585908-7857D768-7724-437A-825B-059F3A7354A7Q28591795-93586F01-4B00-4CBB-8DC7-3FD5F46C4FDFQ30441610-09C8FABB-63E6-4B9C-9F6E-6F9D10CAB005Q30777845-61723D5F-B158-4006-8451-161670FF0822Q33866886-F73247A5-149B-449E-A060-5A530BA13503Q33958096-AD1598D2-CB3B-4CD7-937E-484BAD00EF04Q34036028-514123CC-D636-44FE-8218-12D98BFFF165Q34162432-205F6F85-1366-4793-B526-9BFFC8683094Q34322601-BD3F1813-6A2C-47EE-A3D4-7035BA163161Q34656849-702BB843-DA12-4F0A-AA69-DBC6EFF03CAEQ35103087-1F6310EA-3E1F-4B83-80C0-C7FDB523A39BQ35561006-D86AAAEA-0D34-40F2-BC64-D64C11F2D437Q35591684-90D8D1AE-1FD7-4F94-8227-C1196A19290CQ35881123-4945B3A1-AEC8-46C8-980B-309EAAD7082BQ36001295-D7C6B56D-7C7F-4E32-A0A9-8213DDF967E7Q36326421-B6F2CFEA-C8E4-4673-93EF-5C7DB592E3E8Q36328807-81FB3186-C78E-4B67-8945-1568594891D0Q37213739-BE5BE330-A293-4D0C-A544-92817CDF39D0Q37220425-06F7C93E-8314-49E9-B516-8CD27874D034Q37410050-70C08417-7EF8-4806-8826-D3BE3EB98139Q37497282-D8AAAC77-A5BF-4D30-AA49-CF62443857CDQ37515164-BA4779F9-C315-4CE9-A50E-7B9E418F08F8Q37604084-0A3699F9-BDD0-439F-82DE-4B7889CC01BEQ37775233-8FE45941-5FA2-47D6-BA90-53BC42226EF7Q38265394-F98AB5BF-1387-4AD9-80D9-8F17600CD7BAQ38422083-D5CFCB0E-B92A-4928-9B55-BE029BCB1F52Q38615363-2305CDD6-7BF2-4A25-997D-36A3AC6C5CE4Q38747970-6B591DE9-2BBE-482D-9087-BBB9B54EAFEA
P2860
The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@en
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@nl
type
label
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@en
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@nl
prefLabel
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@en
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@nl
P2093
P1433
P1476
The interaction of the cell-co ...... idylinositol-4,5-bisphosphate.
@en
P2093
Hüttelmaier S
Jockusch BM
Mayboroda O
P304
P356
10.1016/S0960-9822(98)70199-X
P407
P577
1998-04-01T00:00:00Z