Structural and Functional Insights into Human Nuclear Cyclophilins
The peptidyl prolyl isomerases (PPI) of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modification, transcription, and pre-mRNA splicing. This review collects what is kn...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315705/ https://www.ncbi.nlm.nih.gov/pubmed/30518120 http://dx.doi.org/10.3390/biom8040161 |
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author | Rajiv, Caroline Davis, Tara L. |
author_facet | Rajiv, Caroline Davis, Tara L. |
author_sort | Rajiv, Caroline |
collection | PubMed |
description | The peptidyl prolyl isomerases (PPI) of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modification, transcription, and pre-mRNA splicing. This review collects what is known about the eight human nuclear cyclophilins: peptidyl prolyl isomerase H (PPIH), peptidyl prolyl isomerase E (PPIE), peptidyl prolyl isomerase-like 1 (PPIL1), peptidyl prolyl isomerase-like 2 (PPIL2), peptidyl prolyl isomerase-like 3 (PPIL3), peptidyl prolyl isomerase G (PPIG), spliceosome-associated protein CWC27 homolog (CWC27), and peptidyl prolyl isomerase domain and WD repeat-containing protein 1 (PPWD1). Each “spliceophilin” is evaluated in relation to the spliceosomal complex in which it has been studied, and current work studying the biological roles of these cyclophilins in the nucleus are discussed. The eight human splicing complexes available in the Protein Data Bank (PDB) are analyzed from the viewpoint of the human spliceophilins. Future directions in structural and cellular biology, and the importance of developing spliceophilin-specific inhibitors, are considered. |
format | Online Article Text |
id | pubmed-6315705 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63157052019-01-10 Structural and Functional Insights into Human Nuclear Cyclophilins Rajiv, Caroline Davis, Tara L. Biomolecules Review The peptidyl prolyl isomerases (PPI) of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modification, transcription, and pre-mRNA splicing. This review collects what is known about the eight human nuclear cyclophilins: peptidyl prolyl isomerase H (PPIH), peptidyl prolyl isomerase E (PPIE), peptidyl prolyl isomerase-like 1 (PPIL1), peptidyl prolyl isomerase-like 2 (PPIL2), peptidyl prolyl isomerase-like 3 (PPIL3), peptidyl prolyl isomerase G (PPIG), spliceosome-associated protein CWC27 homolog (CWC27), and peptidyl prolyl isomerase domain and WD repeat-containing protein 1 (PPWD1). Each “spliceophilin” is evaluated in relation to the spliceosomal complex in which it has been studied, and current work studying the biological roles of these cyclophilins in the nucleus are discussed. The eight human splicing complexes available in the Protein Data Bank (PDB) are analyzed from the viewpoint of the human spliceophilins. Future directions in structural and cellular biology, and the importance of developing spliceophilin-specific inhibitors, are considered. MDPI 2018-12-04 /pmc/articles/PMC6315705/ /pubmed/30518120 http://dx.doi.org/10.3390/biom8040161 Text en © 2018 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 Rajiv, Caroline Davis, Tara L. Structural and Functional Insights into Human Nuclear Cyclophilins |
title | Structural and Functional Insights into Human Nuclear Cyclophilins |
title_full | Structural and Functional Insights into Human Nuclear Cyclophilins |
title_fullStr | Structural and Functional Insights into Human Nuclear Cyclophilins |
title_full_unstemmed | Structural and Functional Insights into Human Nuclear Cyclophilins |
title_short | Structural and Functional Insights into Human Nuclear Cyclophilins |
title_sort | structural and functional insights into human nuclear cyclophilins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315705/ https://www.ncbi.nlm.nih.gov/pubmed/30518120 http://dx.doi.org/10.3390/biom8040161 |
work_keys_str_mv | AT rajivcaroline structuralandfunctionalinsightsintohumannuclearcyclophilins AT davistaral structuralandfunctionalinsightsintohumannuclearcyclophilins |