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

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–p...

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Detalles Bibliográficos
Autores principales: Hayes, Barbara, van der Geer, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10252698/
https://www.ncbi.nlm.nih.gov/pubmed/37298164
http://dx.doi.org/10.3390/ijms24119214
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author Hayes, Barbara
van der Geer, Peter
author_facet Hayes, Barbara
van der Geer, Peter
author_sort Hayes, Barbara
collection PubMed
description 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.
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spelling pubmed-102526982023-06-10 STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions Hayes, Barbara van der Geer, Peter Int J Mol Sci Review 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. MDPI 2023-05-24 /pmc/articles/PMC10252698/ /pubmed/37298164 http://dx.doi.org/10.3390/ijms24119214 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Hayes, Barbara
van der Geer, Peter
STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title_full STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title_fullStr STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title_full_unstemmed STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title_short STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein–Protein Interactions
title_sort sts-1 and sts-2, multi-enzyme proteins equipped to mediate protein–protein interactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10252698/
https://www.ncbi.nlm.nih.gov/pubmed/37298164
http://dx.doi.org/10.3390/ijms24119214
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