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The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1

RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases are a newly emerging family of phosphatases that are members of DXDX (T/V). The subfamily includes Small CTD phosphatases, like SCP1, SCP2, SCP3, TIMM50, HSPC129 and UBLCP. Extensive study of SCP1 has elicited the diversified roles...

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Autores principales: Reddy R, Harikrishna, Kim, Hackyoung, Noh, Kwangmo, Kim, Young Jun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Biochemistry and Molecular Biology 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4163886/
https://www.ncbi.nlm.nih.gov/pubmed/24755554
http://dx.doi.org/10.5483/BMBRep.2014.47.4.060
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author Reddy R, Harikrishna
Kim, Hackyoung
Noh, Kwangmo
Kim, Young Jun
author_facet Reddy R, Harikrishna
Kim, Hackyoung
Noh, Kwangmo
Kim, Young Jun
author_sort Reddy R, Harikrishna
collection PubMed
description RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases are a newly emerging family of phosphatases that are members of DXDX (T/V). The subfamily includes Small CTD phosphatases, like SCP1, SCP2, SCP3, TIMM50, HSPC129 and UBLCP. Extensive study of SCP1 has elicited the diversified roles of the small C terminal domain phosphatase. The SCP1 plays a vital role in various biological activities, like neuronal gene silencing and preferential Ser5 dephosphorylation, acts as a cardiac hypertrophy inducer with the help of its intronic miRNAs, and has shown a key role in cell cycle regulation. This short review offers an explanation of the mechanism of action of small CTD phosphatases, in different biological activities and metabolic processes. [BMB Reports 2014; 47(4): 192-196]
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spelling pubmed-41638862014-09-16 The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1 Reddy R, Harikrishna Kim, Hackyoung Noh, Kwangmo Kim, Young Jun BMB Rep Review Article RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases are a newly emerging family of phosphatases that are members of DXDX (T/V). The subfamily includes Small CTD phosphatases, like SCP1, SCP2, SCP3, TIMM50, HSPC129 and UBLCP. Extensive study of SCP1 has elicited the diversified roles of the small C terminal domain phosphatase. The SCP1 plays a vital role in various biological activities, like neuronal gene silencing and preferential Ser5 dephosphorylation, acts as a cardiac hypertrophy inducer with the help of its intronic miRNAs, and has shown a key role in cell cycle regulation. This short review offers an explanation of the mechanism of action of small CTD phosphatases, in different biological activities and metabolic processes. [BMB Reports 2014; 47(4): 192-196] Korean Society for Biochemistry and Molecular Biology 2014-04 /pmc/articles/PMC4163886/ /pubmed/24755554 http://dx.doi.org/10.5483/BMBRep.2014.47.4.060 Text en Copyright © 2014, Korean Society for Biochemistry and Molecular Biology http://creativecommons.org/licenses/by-nc/3.0 This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Reddy R, Harikrishna
Kim, Hackyoung
Noh, Kwangmo
Kim, Young Jun
The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title_full The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title_fullStr The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title_full_unstemmed The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title_short The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
title_sort diverse roles of rna polymerase ii c-terminal domain phosphatase scp1
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4163886/
https://www.ncbi.nlm.nih.gov/pubmed/24755554
http://dx.doi.org/10.5483/BMBRep.2014.47.4.060
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