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Publication Type : Journal Article
Publisher : Protein and Cell
Source : Protein and Cell, Volume 2, Number 3, p.237-249 (2011)
Keywords : amino acid sequence, animal cell, Animals, article, cellular distribution, Cercopithecus aethiops, Chlorocebus, controlled study, COS Cells, embryo, HEK293 Cells, human, human cell, Humans, Intracellular Space, microtubule, Microtubules, Models, Molecular, Molecular Sequence Data, nonhuman, Phosphorylation, polyacrylamide gel electrophoresis, priority journal, protein analysis, Protein Binding, protein expression, protein function, protein localization, protein phosphorylation, protein protein interaction, Protein Structure, Rap protein, rap1 GTP-Binding Proteins, Rap1A protein, Ras association domain family protein 1A, Secondary, signal transduction, Substrate Specificity, Tumor Suppressor Proteins, unclassified drug
Department : Medical Oncology
Year : 2011
Abstract : Rap1A is a small G protein implicated in a spectrum of biological processes such as cell proliferation, adhesion, differentiation, and embryogenesis. The downstream effectors through which Rap1A mediates its diverse effects are largely unknown. Here we show that Rap1A, but not the related small G proteins Rap2 or Ras, binds the tumor suppressor Ras association domain family 1A (RASSF1A) in a manner that is regulated by phosphorylation of RASSF1A. Interaction with Rap1A is shown to influence the effect of RASSF1A on microtubule behavior. © Higher Education Press and Springer-Verlag Berlin Heidelberg 2011.
Cite this Research Publication : S. Kab c e Verma, Ganesan, T. Sab f, Kishore, Ug, and Parker, P. Jcd, “The tumor suppressor RASSF1A is a novel effector of small G protein Rap1A”, Protein and Cell, vol. 2, pp. 237-249, 2011.