Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2
about
Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2RhoG signals in parallel with Rac1 and Cdc42Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization.Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamicsPKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindlesStructural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53Formin homology 2 domains occur in multiple contexts in angiospermsMechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectorsThe formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response elementPlasticity-related gene 5 (PRG5) induces filopodia and neurite growth and impedes lysophosphatidic acid- and nogo-A-mediated axonal retractionRegulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complexThe SH3 domain distinguishes the role of I-BAR proteins IRTKS and MIM in chemotactic response to serumNovel isoform of insulin receptor substrate p53/p58 is generated by alternative splicing in the CRIB/SH3-binding region.Entamoeba histolytica encodes unique formins, a subset of which regulates DNA content and cell division.Dynamin1 is a novel target for IRSp53 protein and works with mammalian enabled (Mena) protein and Eps8 to regulate filopodial dynamics.Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain.Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion.Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains.mDia1 and WAVE2 proteins interact directly with IRSp53 in filopodia and are involved in filopodium formationRedundant functions of I-BAR family members, IRSp53 and IRTKS, are essential for embryonic development.Formin' cellular structures: Physiological roles of Diaphanous (Dia) in actin dynamics.Emerging roles for the BAI1 protein family in the regulation of phagocytosis, synaptogenesis, neurovasculature, and tumor development.Membrane shaping by the Bin/amphiphysin/Rvs (BAR) domain protein superfamily.Formins as effector proteins of Rho GTPasesDynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins.An investigation into the potential role of brain angiogenesis inhibitor protein 3 (BAI3) in the tumorigenesis of small-cell carcinoma: a review of the surrounding literature.Rif-mDia1 interaction is involved in filopodium formation independent of Cdc42 and Rac effectors.The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization.mDia1-3 in mammalian filopodia.Control of axon elongation via an SDF-1alpha/Rho/mDia pathway in cultured cerebellar granule neurons.Homo-oligomerization is essential for F-actin assembly by the formin family FH2 domain.
P2860
Q21284173-E7196D7A-B5A6-4E01-A28B-27DCF12375A5Q24310745-BB84A2FB-1D92-4D50-B9F9-A0B0775D912CQ24319871-D0D3C295-F6B6-4031-846B-75B64DBFD67EQ24323192-A465E9A4-DE13-4CD3-9B2A-CF7EAF5FBA8FQ24336730-C5DC9844-A2EB-4254-B1C8-F9DB11378D7BQ24338591-4D5DD42D-5F0D-4BE0-A099-3D063CE20BCBQ24557455-FDF3B10D-F077-4751-B23E-8CCB5866C983Q24797933-2C92B012-E052-45A6-A73E-43B9A3519D16Q27681941-89FBCA2E-5ADF-4FA8-A4A2-631D0B6D37BFQ28190692-39940643-9198-4F49-AF1D-CFC5F091EA21Q28505932-1EF6ACDC-EB7F-4584-9FD1-B00065360155Q28505970-09E23F0C-C6EE-41AF-82DA-8CD289D1960AQ30008854-D6B52ED0-A314-4AD1-A2FB-FD3120B7C28FQ30165426-8717C50A-3AEE-41F1-A66E-0D028E6AC8B8Q30441077-07235980-FA9E-4474-BA2C-4E93E093107AQ30586599-8193362B-E581-4905-83DD-E3CE87D54E36Q31465756-5AD04EBC-5225-4DE1-A401-1285A7947B02Q33455812-0B5B6881-7768-4FCA-9296-4D2BDF2C2639Q34489876-1B488376-4F36-4670-9619-643C95CAF121Q35763102-BB0BC67A-E309-4F45-9C16-36165522856EQ37571307-416F304E-4141-4DCD-B861-27047F759CDEQ37688846-4ADEC6F6-90DA-4F12-AEF1-DE715C47A36FQ37867549-A31C7A8D-9204-498A-8E12-12A0618D79F2Q37902570-C35825AC-7905-4AF5-98EA-AADA5EBF95E1Q38219067-F69721EC-82BD-405F-82BF-4D3CC356AC5CQ38257347-8D29E0F8-AB95-4D9A-97DD-AD6261D8778EQ39325922-973B28AA-B438-42E2-8059-14627FDF62B7Q39588446-3D56ED8D-6AF4-41E6-881B-66E7148F037EQ39673989-C25A4306-CBC6-4EEC-AE1E-31BA687D86AFQ41786923-D57D3B9A-DBD4-42B7-B564-9D95B08480F2Q41830984-7312C015-433F-41BC-8EDF-D6F5944393FFQ45061729-039CFDB3-1BC8-4635-8BEC-D459F4D6E1C1
P2860
Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@ast
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@en
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@nl
type
label
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@ast
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@en
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@nl
prefLabel
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@ast
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@en
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@nl
P2093
P356
P1476
Rho small G-protein-dependent ...... omain-containing IRSp53/BAIAP2
@en
P2093
P356
10.1006/BBRC.2000.2671
P407
P577
2000-05-19T00:00:00Z