(Q52582920)

English

Recruitment of Cdc42 through the GAP domain of RLIP participates in remodeling of the actin cytoskeleton and is involved in Xenopus gastrulation.

scientific article published on 26 September 2007

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scholarly article

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Recruitment of Cdc42 through the GAP domain of RLIP participates in remodeling of the actin cytoskeleton and is involved in Xenopus gastrulation. (English)

1 reference

Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

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Laurent Boissel

1

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Nathalie Houssin

2

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Anissa Chikh

3

1 reference

Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Alla Rynditch

4

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Lucie Van Hove

5

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Jacques Moreau

6

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3 May 2018

http://europepmc.org/abstract/MED/17950267

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26 September 2007

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

Developmental Biology

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3 May 2018

http://europepmc.org/abstract/MED/17950267

312

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

331-343

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

1

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Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

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IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs

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Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity

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FGF signaling restricts the primary blood islands to ventral mesoderm.

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Xbra functions as a switch between cell migration and convergent extension in the Xenopus gastrula

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Ca2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils

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Control of embryonic Xenopus morphogenesis by a Ral-GDS/Xral branch of the Ras signalling pathway.

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RLIP mediates downstream signalling from RalB to the actin cytoskeleton during Xenopus early development

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Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190

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Raf-1 kinase is essential for early Xenopus development and mediates the induction of mesoderm by FGF.

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Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway

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Characterization of Xenopus RalB and its involvement in F-actin control during early development.

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Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis

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Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit

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Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors

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Xenopus Sprouty2 inhibits FGF-mediated gastrulation movements but does not affect mesoderm induction and patterning

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In vivo imaging reveals different cellular functions for FGF and Dpp signaling in tracheal branching morphogenesis

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Rho proteins: linking signaling with membrane trafficking

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The RhoGEF Pebble is required for cell shape changes during cell migration triggered by the Drosophila FGF receptor Heartless.

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Association between GTPase activators for Rho and Ras families.

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Regulation of cortical actin networks in cell migration.

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Involvement of Ras and Ral in chemotactic migration of skeletal myoblasts

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The small G-protein RalA stimulates metastasis of transformed cells.

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Interdependent action of RalGEF and Erk in Ras-induced primitive endoderm differentiation of F9 embryonal carcinoma cells

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Ras caught in another affair: the exchange factors for Ral.

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Identifiers

10.1016/J.YDBIO.2007.09.027

1 reference

Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

1 reference

Europe PubMed Central

3 May 2018

http://europepmc.org/abstract/MED/17950267

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