Literature summary for 2.7.10.2 extracted from

Tong, H.; Zhao, B.; Shi, H.; Ba, X.; Wang, X.; Jiang, Y.; Zeng, X.
c-Abl tyrosine kinase plays a critical role in beta2 integrin-dependent neutrophil migration by regulating Vav1 activity (2013), J. Leukoc. Biol., 93, 611-622.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + Tyr267 of Vav1	-	Homo sapiens	ADP + phosphorylated Tyr267 of Vav1	isoform c-Abl kinase probably regulates the activity of Rho guanine exchange factor Vav1 by direct phosphorylation at Tyr267 in the Dbl homology domain. The C-terminal SH3-SH2-SH3 domain and proline-rich region of Vav1 are required for its interaction with c-Abl kinase	?

Synonyms

Synonyms	Comment	Organism
c-ABL	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	isoform c-Abl kinase is required for neutrophil recruitment in vivo and migration in vitro, and the inhibition of c-Abl kinase activity has a significant impact on neutrophil migratory behavior. c-Abl kinase activation depends on 2 integrin engagement, and the activated c-Abl kinase further regulates actin polymerization and membrane protrusion dynamics at the extended leading edges during neutrophil migration. The Rho guanine exchange factor Vav1 is a major downstream effector of c-Abl kinase. The C-terminal SH3-SH2-SH3 domain and proline-rich region of Vav1 are required for its interaction with c-Abl kinase, and c-Abl kinase probably regulates the activity of Vav1 by direct phosphorylation at Tyr-267 in the Dbl homology domain	Homo sapiens

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Release 2023.1 (January 2023)