NDLI: A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain.

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A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain.

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A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	O'bryan, J. P. Cantley, L. Pawson, T. Der, C. J. Songyang, Z.
Description	Author Affiliation: O'Bryan JP ( Department of Pharmocology, University of North Carolina, Chapel Hill 27599, USA.);
Abstract	The Shc adaptor protein, hereafter referred to as ShcA, possesses two distinct phosphotyrosine-recognition modules, a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated on tyrosine in response to many extracellular signals. Phosphorylation of human ShcA at Tyr-317 within its central (CH1) region induces binding to the Grb2 SH2 domain and is thereby implicated in activation of the Ras pathway. Two shc-related genes (shcB and shcC) have been identified in the mouse. shcB is closely related to human SCK, while shcC has not yet been found in other organisms. The ShcC protein is predicted to have a C-terminal SH2 domain, a CH1 region with a putative Grb2-binding site, and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a specificity related to, but distinct from, that of the ShcA SH2 domain. The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and epidermal growth factor. These results indicate that ShcC has functional SH2 and PTB; domains. In contrast to shcA, which is widely expressed, shcC RNA and proteins are predominantly expressed in the adult brain. These results suggest that ShcC may mediate signaling from tyrosine kinases in the nervous system, such as receptors for neurotrophins.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adaptor Proteins, Signal Transducing Brain Metabolism Neuropeptides Phosphotyrosine Src Homology Domains 3T3 Cells Amino Acid Sequence Animals Binding Sites Cell Line Cloning, Molecular Conserved Sequence DNA Primers Drosophila Mammals Mice Molecular Sequence Data Multigene Family Nerve Tissue Proteins Chemistry Organ Specificity Phosphorylation Polymerase Chain Reaction Protein Biosynthesis Proteins Receptor, Epidermal Growth Factor Receptors, Nerve Growth Factor Recombinant Proteins Biosynthesis Sequence Homology, Amino Acid Shc Signaling Adaptor Proteins Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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