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Targeting the C-Terminal Domain Small Phosphatase 1

The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1’s major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II C...

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Autores principales: Rallabandi, Harikrishna Reddy, Ganesan, Palanivel, Kim, Young Jun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7281111/
https://www.ncbi.nlm.nih.gov/pubmed/32397221
http://dx.doi.org/10.3390/life10050057
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author Rallabandi, Harikrishna Reddy
Ganesan, Palanivel
Kim, Young Jun
author_facet Rallabandi, Harikrishna Reddy
Ganesan, Palanivel
Kim, Young Jun
author_sort Rallabandi, Harikrishna Reddy
collection PubMed
description The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1’s major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II CTD). It is also implicated in various pivotal biological activities, such as acting as a driving factor in repressor element 1 (RE-1)-silencing transcription factor (REST) complex, which silences the neuronal genes in non-neuronal cells, G1/S phase transition, and osteoblast differentiation. Recent findings have denoted that negative regulation of CTDSP1 results in suppression of cancer invasion in neuroglioma cells. Several researchers have focused on the development of regulating materials of CTDSP1, due to the significant roles it has in various biological activities. In this review, we focused on this emerging target and explored the biological significance, challenges, and opportunities in targeting CTDSP1 from a drug designing perspective.
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spelling pubmed-72811112020-06-15 Targeting the C-Terminal Domain Small Phosphatase 1 Rallabandi, Harikrishna Reddy Ganesan, Palanivel Kim, Young Jun Life (Basel) Review The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1’s major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II CTD). It is also implicated in various pivotal biological activities, such as acting as a driving factor in repressor element 1 (RE-1)-silencing transcription factor (REST) complex, which silences the neuronal genes in non-neuronal cells, G1/S phase transition, and osteoblast differentiation. Recent findings have denoted that negative regulation of CTDSP1 results in suppression of cancer invasion in neuroglioma cells. Several researchers have focused on the development of regulating materials of CTDSP1, due to the significant roles it has in various biological activities. In this review, we focused on this emerging target and explored the biological significance, challenges, and opportunities in targeting CTDSP1 from a drug designing perspective. MDPI 2020-05-08 /pmc/articles/PMC7281111/ /pubmed/32397221 http://dx.doi.org/10.3390/life10050057 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Rallabandi, Harikrishna Reddy
Ganesan, Palanivel
Kim, Young Jun
Targeting the C-Terminal Domain Small Phosphatase 1
title Targeting the C-Terminal Domain Small Phosphatase 1
title_full Targeting the C-Terminal Domain Small Phosphatase 1
title_fullStr Targeting the C-Terminal Domain Small Phosphatase 1
title_full_unstemmed Targeting the C-Terminal Domain Small Phosphatase 1
title_short Targeting the C-Terminal Domain Small Phosphatase 1
title_sort targeting the c-terminal domain small phosphatase 1
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7281111/
https://www.ncbi.nlm.nih.gov/pubmed/32397221
http://dx.doi.org/10.3390/life10050057
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