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Signalling through SH2 and SH3 domains.

B J Mayer¹, D Baltimore

¹The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

Trends in Cell Biology

|January 1, 1993

Summary

Researchers discovered the Src homology 2 (SH2) domain in oncogenic tyrosine kinases, crucial for protein interactions. Further studies identified SH3 domains, revealing their role in intracellular signal transduction pathways.

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Area of Science:

Molecular Biology
Cell Signaling
Biochemistry

Background:

The Src homology 2 (SH2) domain was identified in 1986, located outside the catalytic domain of oncogenic tyrosine kinases.
Subsequent research revealed a second homologous region, the SH3 domain, in various proteins.

Purpose of the Study:

To investigate the function of newly identified protein homology regions, SH2 and SH3 domains.
To understand the role of these domains in protein-protein interactions and intracellular signaling.

Main Methods:

Comparative sequence analysis to identify homologous regions in proteins.
Protein interaction studies to elucidate the function of SH2 and SH3 domains.

Main Results:

SH2 and SH3 domains were found to mediate controlled protein-protein interactions.
Proteins containing SH2 and SH3 domains are frequently involved in signal transduction.

Conclusions:

The discovery of SH2 and SH3 domains provides insights into the regulation of intracellular signaling pathways.
These domains represent a key mechanism for controlling signal transduction in cells.

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