Views and Reviews Tyrosine Protein Kinase Substrate p 36 : A Member of the Annexin Family of Ca 2 - I - / P hosphol ipid - Bindi ng Proteins
نویسنده
چکیده
Ten years ago a protein of apparent M, 36,000 was identified as a major cellular target for the transforming tyrosine kinase encoded by the src oncogene. In a series of in vivo labeling experiments, Radke and Martin [1979], Radke et al. [1980], and Erikson and Erikson [1980] showed that p36 is phosphorylated on tyrosine residues when chicken embryo fibroblasts are transformed by Rous sarcoma virus. This finding sparked much interest in p36 and initiated the search for its cellular function(s). Several studies proposed a role in membrane-cytoskeleton interactions, membrane fusion, or signal transduction. While the exact physiological role of this pp60"" substrate is still unclear, intensive research has led to a detailed biochemical and structural characterization of p36, which will be discussed in this review.
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The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites.
Annexin II, a member of the annexin family of Ca(2+)- and lipid-binding proteins, is a major substrate of the pp60src kinase. It is unique within the annexin protein family, since it can form a tight heterotetrameric complex with the cellular protein ligand p11, a member of the S100 protein family. Within the cell, the annexin II2p11(2) complex is localized at the cytoplasmic surface of the pla...
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