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Alternative splicing regulation by interaction of phosphatase PP2Cγ with nucleic acid–binding protein YB-1

Overview of attention for article published in Nature Structural & Molecular Biology, June 2007
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About this Attention Score

  • Good Attention Score compared to outputs of the same age (66th percentile)

Mentioned by

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1 Wikipedia page

Citations

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46 Dimensions

Readers on

mendeley
39 Mendeley
Title
Alternative splicing regulation by interaction of phosphatase PP2Cγ with nucleic acid–binding protein YB-1
Published in
Nature Structural & Molecular Biology, June 2007
DOI 10.1038/nsmb1257
Pubmed ID
Authors

Eric Allemand, Michelle L Hastings, Michael V Murray, Michael P Myers, Adrian R Krainer

Abstract

Kinases and phosphatases participate in precursor messenger RNA (pre-mRNA) splicing regulation, but their precise roles and the identities of their cofactors and substrates remain poorly understood. The human Ser/Thr phosphatase PP2Cgamma promotes spliceosome assembly. We show that PP2Cgamma's distinctive acidic domain is essential for its activity in splicing and interacts with YB-1, a spliceosome-associated factor. Moreover, PP2Cgamma is a phosphoprotein in vivo, and its acidic domain is phosphorylated under splicing conditions in vitro. PP2Cgamma phosphorylation enhances its interaction with YB-1 and is reversed by the phosphatase in cis. PP2Cgamma knockdown leaves constitutive splicing unaffected but inhibits cell proliferation and affects alternative splicing of CD44, a YB-1 target. This effect on splicing regulation is mediated by PP2Cgamma's acidic domain, which is essential to promote inclusion of CD44 exons v4 and v5 in vivo. We propose that PP2Cgamma modulates alternative splicing of specific pre-mRNAs coregulated by YB-1.

Mendeley readers

The data shown below were compiled from readership statistics for 39 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 3%
Argentina 1 3%
Unknown 37 95%

Demographic breakdown

Readers by professional status Count As %
Researcher 15 38%
Student > Ph. D. Student 11 28%
Professor 3 8%
Professor > Associate Professor 2 5%
Student > Master 2 5%
Other 3 8%
Unknown 3 8%
Readers by discipline Count As %
Agricultural and Biological Sciences 24 62%
Biochemistry, Genetics and Molecular Biology 9 23%
Medicine and Dentistry 2 5%
Sports and Recreations 1 3%
Unknown 3 8%

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 January 2008.
All research outputs
#3,622,451
of 12,482,173 outputs
Outputs from Nature Structural & Molecular Biology
#1,274
of 2,420 outputs
Outputs of similar age
#79,077
of 271,201 outputs
Outputs of similar age from Nature Structural & Molecular Biology
#39
of 51 outputs
Altmetric has tracked 12,482,173 research outputs across all sources so far. This one is in the 49th percentile – i.e., 49% of other outputs scored the same or lower than it.
So far Altmetric has tracked 2,420 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 10.2. This one is in the 31st percentile – i.e., 31% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 271,201 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 66% of its contemporaries.
We're also able to compare this research output to 51 others from the same source and published within six weeks on either side of this one. This one is in the 23rd percentile – i.e., 23% of its contemporaries scored the same or lower than it.