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Phosphorylated guanine nucleotide exchange factor C3G, induced by pervanadate and Src family kinases localizes to the Golgi and subcortical actin cytoskeleton by Vegesna Radha; Ajumeera Rajanna; Ghanshyam Swarup is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Background The guanine nucleotide exchange factor C3G (RapGEF1) along with its effector proteins participates in signaling pathways that regulate eukaryotic cell proliferation, adhesion, apoptosis and embryonic development. It activates Rap1, Rap2 and R-Ras members of the Ras family of GTPases. C3G is activated upon phosphorylation at tyrosine 504 and therefore, determining the localization of phosphorylated C3G would provide an insight into its site of action in the cellular context. ## Results C3G is phosphorylated in vivo on Y504 upon coexpression with Src or Hck, two members of the Src family tyrosine kinases. Here we have determined the subcellular localization of this protein using antibodies specific to C3G and Tyr 504 phosphorylated C3G (pY504 C3G). While exogenously expressed C3G was present mostly in the cytosol, pY504 C3G formed upon Hck or Src coexpression localized predominantly at the cell membrane and the Golgi complex. Tyrosine 504-phosphorylated C3G showed colocalization with Hck and Src. Treatment of Hck and C3G transfected cells with pervanadate showed an increase in the cytosolic staining of pY504 C3G suggesting that tyrosine phosphatases may be involved in d

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Author

Vegesna Radha; Ajumeera Rajanna; Ghanshyam Swarup

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central, [2000]-2018.; Springer Science and Business Media LLC (ISSN 1471-2121)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)