Evidence map›Paper›PMID 29851470›Full record

ArticleBiochemistry2018

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

Jeffrey M Pina, Janice M Reynaga, Anthony A M Truong, Niroshika M Keppetipola

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 30 citations in OpenAlex.

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  6. Cpeb4-mediated Dclk2 promotes neuronal pyroptosis induced by chronic cerebral ischemia through phosphorylation of Ehf.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Jeffrey M PinaDepartment of Chemistry and Biochemistry , California State University, Fullerton , 800 North State College Boulevard , Fullerton , California 92831 , United States.
Janice M ReynagaDepartment of Chemistry and Biochemistry , California State University, Fullerton , 800 North State College Boulevard , Fullerton , California 92831 , United States.
Anthony A M TruongDepartment of Chemistry and Biochemistry , California State University, Fullerton , 800 North State College Boulevard , Fullerton , California 92831 , United States.
Niroshika M KeppetipolaDepartment of Chemistry and Biochemistry , California State University, Fullerton , 800 North State College Boulevard , Fullerton , California 92831 , United States.ORCID 0000-0001-9848-2906
California State University, Fullerton · US

Funding

MARC PROGRAM FOR CALIFORNIA STATE UNIVERSITY, FULLERTONT34GM008612 · NIGMS · CALIFORNIA STATE UNIVERSITY FULLERTON · PI COHEN, AMYBETH · 1996 to 2021
$7.4M
NIGMS NIH HHS T34 GM008612
6 · The paper itself

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.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid MotifsEscherichia coliHeterogeneous-Nuclear RibonucleoproteinsHumansNerve Tissue ProteinsPhosphorylationPolypyrimidine Tract-Binding ProteinRecombinant ProteinsHeterogeneous-Nuclear RibonucleoproteinsNerve Tissue ProteinsPolypyrimidine Tract-Binding ProteinPTBP1 protein, humanPTBP2 protein, humanRecombinant Proteins

Identifiers

PMID29851470
PMCPMC6211845
OpenAlexW2806290836

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.