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TRIM22: A Diverse and Dynamic Antiviral Protein
The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signature...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356915/ https://www.ncbi.nlm.nih.gov/pubmed/22649727 http://dx.doi.org/10.1155/2012/153415 |
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author | Hattlmann, Clayton J. Kelly, Jenna N. Barr, Stephen D. |
author_facet | Hattlmann, Clayton J. Kelly, Jenna N. Barr, Stephen D. |
author_sort | Hattlmann, Clayton J. |
collection | PubMed |
description | The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signatures of positive selection. To date, TRIM22 has been shown to restrict the replication of a number of viruses, including encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1). In addition, TRIM22 has also been implicated in cellular differentiation and proliferation and may play a role in certain cancers and autoimmune diseases. This comprehensive paper summarizes our current understanding of TRIM22 structure and function. |
format | Online Article Text |
id | pubmed-3356915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-33569152012-05-30 TRIM22: A Diverse and Dynamic Antiviral Protein Hattlmann, Clayton J. Kelly, Jenna N. Barr, Stephen D. Mol Biol Int Review Article The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signatures of positive selection. To date, TRIM22 has been shown to restrict the replication of a number of viruses, including encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1). In addition, TRIM22 has also been implicated in cellular differentiation and proliferation and may play a role in certain cancers and autoimmune diseases. This comprehensive paper summarizes our current understanding of TRIM22 structure and function. Hindawi Publishing Corporation 2012 2012-05-08 /pmc/articles/PMC3356915/ /pubmed/22649727 http://dx.doi.org/10.1155/2012/153415 Text en Copyright © 2012 Clayton J. Hattlmann et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Hattlmann, Clayton J. Kelly, Jenna N. Barr, Stephen D. TRIM22: A Diverse and Dynamic Antiviral Protein |
title | TRIM22: A Diverse and Dynamic Antiviral Protein |
title_full | TRIM22: A Diverse and Dynamic Antiviral Protein |
title_fullStr | TRIM22: A Diverse and Dynamic Antiviral Protein |
title_full_unstemmed | TRIM22: A Diverse and Dynamic Antiviral Protein |
title_short | TRIM22: A Diverse and Dynamic Antiviral Protein |
title_sort | trim22: a diverse and dynamic antiviral protein |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356915/ https://www.ncbi.nlm.nih.gov/pubmed/22649727 http://dx.doi.org/10.1155/2012/153415 |
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