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Versatile communication strategies among tandem WW domain repeats

Interactions mediated by short linear motifs in proteins play major roles in regulation of cellular homeostasis since their transient nature allows for easy modulation. We are still far from a full understanding and appreciation of the complex regulation patterns that can be, and are, achieved by th...

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Autores principales: Dodson, Emma Joy, Fishbain-Yoskovitz, Vered, Rotem-Bamberger, Shahar, Schueler-Furman, Ora
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436281/
https://www.ncbi.nlm.nih.gov/pubmed/25710931
http://dx.doi.org/10.1177/1535370214566558
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author Dodson, Emma Joy
Fishbain-Yoskovitz, Vered
Rotem-Bamberger, Shahar
Schueler-Furman, Ora
author_facet Dodson, Emma Joy
Fishbain-Yoskovitz, Vered
Rotem-Bamberger, Shahar
Schueler-Furman, Ora
author_sort Dodson, Emma Joy
collection PubMed
description Interactions mediated by short linear motifs in proteins play major roles in regulation of cellular homeostasis since their transient nature allows for easy modulation. We are still far from a full understanding and appreciation of the complex regulation patterns that can be, and are, achieved by this type of interaction. The fact that many linear-motif-binding domains occur in tandem repeats in proteins indicates that their mutual communication is used extensively to obtain complex integration of information toward regulatory decisions. This review is an attempt to overview, and classify, different ways by which two and more tandem repeats cooperate in binding to their targets, in the well-characterized family of WW domains and their corresponding polyproline ligands.
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spelling pubmed-44362812015-05-19 Versatile communication strategies among tandem WW domain repeats Dodson, Emma Joy Fishbain-Yoskovitz, Vered Rotem-Bamberger, Shahar Schueler-Furman, Ora Exp Biol Med (Maywood) Minireviews Interactions mediated by short linear motifs in proteins play major roles in regulation of cellular homeostasis since their transient nature allows for easy modulation. We are still far from a full understanding and appreciation of the complex regulation patterns that can be, and are, achieved by this type of interaction. The fact that many linear-motif-binding domains occur in tandem repeats in proteins indicates that their mutual communication is used extensively to obtain complex integration of information toward regulatory decisions. This review is an attempt to overview, and classify, different ways by which two and more tandem repeats cooperate in binding to their targets, in the well-characterized family of WW domains and their corresponding polyproline ligands. SAGE Publications 2015-03 /pmc/articles/PMC4436281/ /pubmed/25710931 http://dx.doi.org/10.1177/1535370214566558 Text en © 2015 by the Society for Experimental Biology and Medicine http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 3.0 License (http://www.creativecommons.org/licenses/by-nc/3.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access page(http://www.uk.sagepub.com/aboutus/openaccess.htm).
spellingShingle Minireviews
Dodson, Emma Joy
Fishbain-Yoskovitz, Vered
Rotem-Bamberger, Shahar
Schueler-Furman, Ora
Versatile communication strategies among tandem WW domain repeats
title Versatile communication strategies among tandem WW domain repeats
title_full Versatile communication strategies among tandem WW domain repeats
title_fullStr Versatile communication strategies among tandem WW domain repeats
title_full_unstemmed Versatile communication strategies among tandem WW domain repeats
title_short Versatile communication strategies among tandem WW domain repeats
title_sort versatile communication strategies among tandem ww domain repeats
topic Minireviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436281/
https://www.ncbi.nlm.nih.gov/pubmed/25710931
http://dx.doi.org/10.1177/1535370214566558
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