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Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2.

Abstract：

:RNA binding proteins play an important role in regulating alternative pre-mRNA splicing and in turn cellular gene expression. Many of these RNA binding proteins occur as gene families with members sharing a high degree of primary structure identity and domain organization yet have tissue-specific expression patterns and regulate different sets of target exons. How highly similar members in a gene family can exert different splicing outcomes is not well understood. We conducted mass spectrometry analysis of post-translational phosphorylation and acetylation modifications for two paralogs of the polypyrimidine tract binding protein family, PTBP1 and PTBP2, to discover modifications that occur in splicing reaction mixtures and to identify discrete modifications that may direct their different splicing activities. We find that PTBP1 and PTBP2 have many distinct phosphate modifications located in the unstructured N-terminal, linker 1, and linker 2 regions. We find that the two proteins have many overlapping acetate modifications in the RNA recognition motifs (RRMs) with a few distinct sites in PTBP1 RRM2 and RRM3. Our data also reveal that lysine residues in the nuclear localization sequence of PTBP2 are acetylated. Collectively, our results highlight important differences in post-translational modifications between the paralogs and suggest a role for them in the differential splicing activity of PTBP1 and PTBP2.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Pina JM,Reynaga JM,Truong AAM,Keppetipola NM

doi

10.1021/acs.biochem.8b00256

subject

Has Abstract

pub_date

2018-07-03 00:00:00

pages

3873-3882

issue

26

eissn

0006-2960

issn

1520-4995

journal_volume

57

pub_type

杂志文章

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