Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
about
Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeletonIntegrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagementProteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading.The cytoplasmic domain of the integrin alpha9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent mannerThe role of vascular cell adhesion molecule-1 in tumor immune evasionSpermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migrationActopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesionT Lymphocyte Migration: An Action Movie Starring the Actin and Associated Actors.Leukocyte integrins: role in leukocyte recruitment and as therapeutic targets in inflammatory diseaseInflammatory pathways of importance for management of inflammatory bowel diseaseNMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding modelNMR solution conformations and interactions of integrin alphaLbeta2 cytoplasmic tailsStructures and Interaction Analyses of Integrin M 2 Cytoplasmic TailsCharacterization of 14-3-3-ζ Interactions with Integrin TailsAlpha4 integrins and the immune responseA fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migrationIncreased filamin binding to beta-integrin cytoplasmic domains inhibits cell migrationPhosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin bindingMiro-1 links mitochondria and microtubule Dynein motors to control lymphocyte migration and polarity.Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillinalpha1 Integrin cytoplasmic domain is involved in focal adhesion formation via association with intracellular proteinsNMR structure of integrin α4 cytosolic tail and its interactions with paxillinLinkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytesNischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migrationPlasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141Syndecan-4 associates with alpha-actininThe adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signalingProteomic analysis of α4β1 integrin adhesion complexes reveals α-subunit-dependent protein recruitmentSusceptibility loci associated with specific and shared subtypes of lymphoid malignanciesPaxillin: a focal adhesion-associated adaptor protein.Distinct signaling mechanisms regulate migration in unconfined versus confined spacesLive cell imaging of paxillin in rolling neutrophils by dual-color quantitative dynamic footprintingSelective modulation of integrin-mediated cell migration by distinct ADAM family membersThe LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL).Targeting Pyk2 to beta 1-integrin-containing focal contacts rescues fibronectin-stimulated signaling and haptotactic motility defects of focal adhesion kinase-null cellsalpha4beta1 integrin regulates lamellipodia protrusion via a focal complex/focal adhesion-independent mechanism.Integrin alpha4beta1 promotes focal adhesion kinase-independent cell motility via alpha4 cytoplasmic domain-specific activation of c-Src.The critical cytoplasmic regions of the alphaL/beta2 integrin in Rap1-induced adhesion and migration.Alpha4beta1 integrin/ligand interaction inhibits alpha5beta1-induced stress fibers and focal adhesions via down-regulation of RhoA and induces melanoma cell migration.
P2860
Q22254255-A2630C99-6EEB-42D7-807A-AAD6E5F0C528Q24292725-9415743D-787C-4545-ACCF-25DAB3BA86C8Q24314482-2130CC4B-ED26-4636-A5D2-DCA7D55757B8Q24319896-774DA47D-343A-48D5-A043-91A2DDAF08DFQ24555127-A59228EF-BC42-4B05-A28A-69FB3F1DBAAAQ24635847-8BA7B4D6-9BD4-40B5-AAF5-E92D019F41DEQ24676154-F5091101-F7EA-4A85-91F2-1C4695EC3520Q24685749-D65941BA-4048-492D-885A-C40BB755E353Q26774663-E93DF786-D96F-4109-808E-97463512FA31Q26822941-CBD08B1E-B12A-42F6-841B-B73FA31640CAQ27005445-C8B06EDF-9E4C-465F-82A4-759ECBA7044AQ27642755-74534B59-CD23-4BD9-820C-AF43D0718887Q27653113-C01CAEE9-3964-46B8-9BC9-77A3EBB0713EQ27675372-A4053B3F-22CA-47B3-B089-5FE144BB9AA8Q27678611-46ECD0B3-AB9C-4FF8-92B5-0EDC7FD6DF5EQ28202046-4FC954C6-D391-471C-9E50-788A5ACA4014Q28210855-09B7FA52-1789-4D4B-9C56-0B0073F06929Q28214955-5CCA73B8-830D-4B92-A4EF-A7A91D5B022AQ28215040-49E3F31C-3EF9-4993-902C-3AFF84D99246Q28307218-7EBB10E5-E3A8-44CE-AFB0-FFDB1FF5E922Q28363290-963B144B-96C0-42F8-A831-B7A9080F2AD1Q28364295-FAEEC994-ADE6-4EB1-A5A7-F7462EABE903Q28485876-5F42D976-169D-433F-BB09-66980AC122EDQ28508545-31A327EC-7039-44AA-9753-BBF500AFDA80Q28509897-271403E8-FDFA-488C-88E9-8A0FEEF9205CQ28546343-1FFDD838-ABA0-47BC-9B15-7D2DB70611A4Q28565623-F10384FA-7C4A-449C-A429-E8639CE5365BQ28589349-1523D6AF-23E6-4210-B51E-7D688F09AA5AQ28727031-4E8BA63B-2B60-4BA6-B1E5-C10328E6FA65Q28943260-965BD896-98B2-45C5-B13A-5578BC96E5EFQ30167845-DEB91165-1A2E-42E0-9611-6A6ED1A4521DQ30414448-DED54541-15A7-4747-8D96-25C836D6FA78Q30426233-7DF1B44B-2DD8-42D9-B77C-2269BBBC7C5DQ30437660-B5C6CD80-F438-4395-AA6F-516ADBDE185AQ30441975-28156BFC-7FCE-48D2-B20E-5FE31A6FD556Q30442000-93AAC21D-1DC2-48CA-B5DF-BADF1FA2ABEAQ30476231-811580B6-A636-42DD-8156-0764C4B8F4BEQ30476291-6D3A68AA-FDC7-4073-B721-295871859ADFQ30479889-720B2BAD-4030-4017-A5CE-8BEB37E79DCCQ30480029-73F25DF1-7155-4C8A-8A8F-926C1AE002BC
P2860
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@ast
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en-gb
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@nl
type
label
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@ast
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en-gb
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@nl
prefLabel
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@ast
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en-gb
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@nl
P2093
P356
P1433
P1476
Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
@en
P2093
D G Woodside
M H Ginsberg
S M Thomas
W B Kiosses
P2888
P304
P356
10.1038/45264
P407
P577
1999-12-09T00:00:00Z
P6179
1019013386