(Q24313265)

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Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase. Role of Rho family small GTPases

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Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase. Role of Rho family small GTPases (English)

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EPH receptor B3

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GOA release 2020-03-11

ephrin receptor signaling pathway

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GOA release 2020-03-11

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based on heuristic

inferred from title

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based on heuristic

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author name string

Hui Miao

1

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Klaus Strebhardt

2

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Elena B Pasquale

3

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Tang-Long Shen

4

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Jun-Lin Guan

5

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Bingcheng Wang

6

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language of work or name

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publication date

14 January 2005

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Journal of Biological Chemistry

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280

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2

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923-32

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The protein kinase complement of the human genome

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Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis

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Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling

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Tyrosine phosphorylation of transmembrane ligands for Eph receptors

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The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans

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Kinase-independent requirement of EphB2 receptors in hippocampal synaptic plasticity

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Kinase-dependent and kinase-independent functions of EphA4 receptors in major axon tract formation in vivo.

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Nuk controls pathfinding of commissural axons in the mammalian central nervous system

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Integrins regulate Rac targeting by internalization of membrane domains

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The mouse kinome: discovery and comparative genomics of all mouse protein kinases

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PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor

1 reference

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Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity

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EphA kinase activation regulates HGF-induced epithelial branching morphogenesis

1 reference

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Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta

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Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton

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Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase

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An Eph receptor regulates integrin activity through R-Ras

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Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells

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Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity

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RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity

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Interplay between Rac and Rho in the control of substrate contact dynamics

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Redox-dependent downregulation of Rho by Rac.

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Regulation of repulsion versus adhesion by different splice forms of an Eph receptor

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Cross-linking of EphB6 resulting in signal transduction and apoptosis in Jurkat cells

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Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses

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EphA3 is induced by CD28 and IGF-1 and regulates cell adhesion.

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Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI

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based on heuristic

inferred from DOI database lookup

Multiple ephrins control cell organization in C. elegans using kinase-dependent and -independent functions of the VAB-1 Eph receptor

1 reference

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based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.M411383200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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