Protein phosphatase 2A family members (PP2A and PP6) associate with U1 snRNP and the spliceosome during pre-mRNA splicing

Kamoun, Malek, Filali, Mohammed, Murray, Michael V., Awasthi, Sita, Wadzinski, Brian E. (October 2013) Protein phosphatase 2A family members (PP2A and PP6) associate with U1 snRNP and the spliceosome during pre-mRNA splicing. Biochemical and Biophysical Research Communications, 440 (2). pp. 306-311. ISSN 0006-291X

URL: https://www.ncbi.nlm.nih.gov/pubmed/24064353
DOI: 10.1016/j.bbrc.2013.09.068

Abstract

Abstract Protein phosphorylation and dephosphorylation are both important for multiple steps in the splicing pathway. Members of the PP1 and PP2A subfamilies of phospho-serine/threonine phosphatases play essential but redundant roles in the second step of the splicing reaction. PP6, a member of the PP2A subfamily, is the mammalian homologue of yeast Sit4p and ppe1, which are involved in cell cycle regulation; however, the involvement of PP6 in the splicing pathway remains unclear. Here we show that PP2A family members physically associate with the spliceosome throughout the splicing reaction. PP2A holoenzyme and PP6 were found stably associated with U1 snRNP. Together our findings indicate that these phosphatases regulate splicing catalysis involving U1 snRNP and suggest an important evolutionary conserved role of PP2A family phosphatases in pre-mRNA splicing.

Item Type: Paper
Uncontrolled Keywords: PP2A PP6 phosphatase snRNPs pre-mRNA splicing
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > spliceosome complex
CSHL Authors:
Communities: CSHL labs > Krainer lab
Depositing User: Matt Covey
Date: 18 October 2013
Date Deposited: 25 Sep 2013 15:20
Last Modified: 21 Feb 2018 17:07
PMCID: PMC3891829
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28631

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