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Cited by 1,868

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins

Koch, C. Anne, Anderson, Deborah, Moran, Michael F., Ellis, Christine, Pawson, Tony·1991·Science
DOI 10.1126/science.1708916
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Abstract

Src homology (SH) regions 2 and 3 are noncatalytic domains that are conserved among a series of cytoplasmic signaling proteins regulated by receptor protein-tyrosine kinases, including phospholipase C-γ, Ras GTPase (guanosine triphosphatase)-activating protein, and Src-like tyrosine kinases. The SH2 domains of these signaling proteins bind tyrosine phosphorylated polypeptides, implicated in normal signaling and cellular transformation. Tyrosine phosphorylation acts as a switch to induce the binding of SH2 domains, thereby mediating the formation of heteromeric protein complexes at or near the plasma membrane. The formation of these complexes is likely to control the activation of signal transduction pathways by tyrosine kinases. The SH3 domain is a distinct motif that, together with SH2, may modulate interactions with the cytoskeleton and membrane. Some signaling and transforming proteins contain SH2 and SH3 domains unattached to any known catalytic element. These noncatalytic proteins may serve as adaptors to link tyrosine kinases to specific target proteins. These observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.

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Metadata

Authors
Koch, C. A., Anderson, D., Moran, M. F., Ellis, C., & Pawson, T.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1991-05-03
Volume
252
Issue
5006
Pages
668-674
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1708916
OpenAlex
W2038816853
Cited by
1,868
References
3
FWCI
104.77
Type
journal article
Language
en
Open access
closed

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