Description
Rap1A is a 21 kDa small GTP-binding protein that antagonizes the Ras transforming activity through tight binding to Ras-GAP. It interferes with Ras-dependent Raf1 activation by inhibiting binding of Ras to the cysteine-rich region of Raf1. This protein is localized in the endoplasmic reticulum, late endosomes, and lysosomes, indicating its potential role in the regulation of intracellular protein degradation. Rap1a contains a C-terminal CLLL motif for post-translational geranylgeranylation and a single site for phosphorylation by protein kinase A. Ras proteins provide a crucial link in the intracellular signalling cascades. Ras proteins are members of the small G protein family. These proteins are characterized by a molecular weight between 20 and 30 kDa, the ability to bind GTP or GDP and a low intrinsic GTPase activity. These proteins relay signals from the plasma membrane activated by receptor tyrosine kinases to the nucleus via a network of serine/threonine kinases. Ras proteins belong to a family of approximately 40 mammalian and 60 non-mammalian proteins. Ras proteins were first discovered as the hyperactive products of mutant Ras genes which promote cancer by disrupting the normal controls on cell proliferation and differentiation; about 30% of human cancers have mutations in a Ras gene