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Review
. 2023 May 24;24(11):9214.
doi: 10.3390/ijms24119214.

STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein-Protein Interactions

Barbara Hayes  1 , Peter van der Geer  1
Affiliations
Review

STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein-Protein Interactions

Barbara Hayes et al. Int J Mol Sci. .

Abstract

STS-1 and STS-2 form a small family of proteins that are involved in the regulation of signal transduction by protein-tyrosine kinases. Both proteins are composed of a UBA domain, an esterase domain, an SH3 domain, and a PGM domain. They use their UBA and SH3 domains to modify or rearrange protein-protein interactions and their PGM domain to catalyze protein-tyrosine dephosphorylation. In this manuscript, we discuss the various proteins that have been found to interact with STS-1 or STS-2 and describe the experiments used to uncover their interactions.

Keywords: BCR-ABL1; Cbl; EGF receptor; SH3; STS-1; STS-2; protein–tyrosine kinases.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic representation of STS-1 and STS-2.
See this image and copyright information in PMC

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