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Ser/Thr protein phosphatases in fungi: structure, regulation and function
Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, col...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Shared Science Publishers OG
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6506691/ https://www.ncbi.nlm.nih.gov/pubmed/31114794 http://dx.doi.org/10.15698/mic2019.05.677 |
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author | Ariño, Joaquín Velázquez, Diego Casamayor, Antonio |
author_facet | Ariño, Joaquín Velázquez, Diego Casamayor, Antonio |
author_sort | Ariño, Joaquín |
collection | PubMed |
description | Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, collectively called Ser/Thr protein phosphatases. The activity of these enzymes has an enormous impact on cellular functioning. In this work we pre-sent the members of this family in S. cerevisiae and other fungal species, and review the most recent findings concerning their regu-lation and the roles they play in the most diverse aspects of cell biology. |
format | Online Article Text |
id | pubmed-6506691 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Shared Science Publishers OG |
record_format | MEDLINE/PubMed |
spelling | pubmed-65066912019-05-21 Ser/Thr protein phosphatases in fungi: structure, regulation and function Ariño, Joaquín Velázquez, Diego Casamayor, Antonio Microb Cell Review Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, collectively called Ser/Thr protein phosphatases. The activity of these enzymes has an enormous impact on cellular functioning. In this work we pre-sent the members of this family in S. cerevisiae and other fungal species, and review the most recent findings concerning their regu-lation and the roles they play in the most diverse aspects of cell biology. Shared Science Publishers OG 2019-04-24 /pmc/articles/PMC6506691/ /pubmed/31114794 http://dx.doi.org/10.15698/mic2019.05.677 Text en https://creativecommons.org/licenses/by/4.0/ This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged. |
spellingShingle | Review Ariño, Joaquín Velázquez, Diego Casamayor, Antonio Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title | Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title_full | Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title_fullStr | Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title_full_unstemmed | Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title_short | Ser/Thr protein phosphatases in fungi: structure, regulation and function |
title_sort | ser/thr protein phosphatases in fungi: structure, regulation and function |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6506691/ https://www.ncbi.nlm.nih.gov/pubmed/31114794 http://dx.doi.org/10.15698/mic2019.05.677 |
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