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Sci. STKE, 15 July 2003
Vol. 2003, Issue 191, p. re12
[DOI: 10.1126/stke.2003.191.re12]

REVIEWS

SH2 and PTB Domains in Tyrosine Kinase Signaling

Joseph Schlessinger1* and Mark A. Lemmon2

1Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.
2Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Gloss: With five figures and 122 citations, this STKE Review describes protein motifs that recognize amino acid sequences that contain phosphorylated tyrosines, the Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains. SH2 and PTB domains are small protein modules that function as key building blocks of the intracellular circuitry that is necessary for signal transmission from the cell surface to different parts of the living cell. Although initially identified as modules that recognize phosphorylated tyrosines, subsequent studies indicated that only binding of SH2 domains to their target proteins is strictly regulated by tyrosine phosphorylation, whereas most PTB domains actually bind to their (nonphosphorylated) targets constitutively. SH2 and PTB domains control proteins' cellular localization, protein assembly and dimerization, and protein activation. Proteins containing PTB or SH2 domains contribute to the regulation of cell cycle, cell shape and movement, cell differentiation, and cell survival.

*Corresponding author. Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, SHM B-204, New Haven, CT 06520, USA. Telephone, (203) 785-7395; e-mail, joseph.schlessinger{at}yale.edu

Citation: J. Schlessinger, M. A. Lemmon, SH2 and PTB Domains in Tyrosine Kinase Signaling. Sci. STKE 2003, re12 (2003).

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Combinatorial ShcA Docking Interactions Support Diversity in Tissue Morphogenesis.
W. R. Hardy, L. Li, Z. Wang, J. Sedy, J. Fawcett, E. Frank, J. Kucera, and T. Pawson (2007)
Science 317, 251-256
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