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Advances in the Study of SR Protein Family

The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS d...

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Detalles Bibliográficos
Autores principales: Ma, Xiaoyun, He, Fuchu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172405/
https://www.ncbi.nlm.nih.gov/pubmed/15626328
http://dx.doi.org/10.1016/S1672-0229(03)01002-7
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author Ma, Xiaoyun
He, Fuchu
author_facet Ma, Xiaoyun
He, Fuchu
author_sort Ma, Xiaoyun
collection PubMed
description The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms for alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation.
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spelling pubmed-51724052016-12-23 Advances in the Study of SR Protein Family Ma, Xiaoyun He, Fuchu Genomics Proteomics Bioinformatics Review The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms for alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation. Elsevier 2003-02 2016-11-28 /pmc/articles/PMC5172405/ /pubmed/15626328 http://dx.doi.org/10.1016/S1672-0229(03)01002-7 Text en . http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review
Ma, Xiaoyun
He, Fuchu
Advances in the Study of SR Protein Family
title Advances in the Study of SR Protein Family
title_full Advances in the Study of SR Protein Family
title_fullStr Advances in the Study of SR Protein Family
title_full_unstemmed Advances in the Study of SR Protein Family
title_short Advances in the Study of SR Protein Family
title_sort advances in the study of sr protein family
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172405/
https://www.ncbi.nlm.nih.gov/pubmed/15626328
http://dx.doi.org/10.1016/S1672-0229(03)01002-7
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