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Vimentin dephosphorylation at ser-56 is regulated by type 1 protein phosphatase in smooth muscle

Overview of attention for article published in Respiratory Research, July 2016
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Title
Vimentin dephosphorylation at ser-56 is regulated by type 1 protein phosphatase in smooth muscle
Published in
Respiratory Research, July 2016
DOI 10.1186/s12931-016-0415-7
Pubmed ID
Authors

Jia Li, Ruping Wang, Dale D. Tang

Abstract

The intermediate filament protein vimentin undergoes reversible phosphorylation and dephosphorylation at Ser-56, which plays an important role in regulating the contraction-relaxation cycles of smooth muscle. The protein phosphatases that mediate vimentin dephosphorylation in smooth muscle have not been previously investigated. The associations of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) with vimentin in mouse tracheal rings was evaluated by co-immunoprecipitation. Lentivirus-mediated shRNA against PP1 was used to assess the role of PP1 in vimentin dephosphorylation and the vimentin-associated process in smooth muscle. Co-immunoprecipitation analysis showed that vimentin interacted with PP1, but barely with PP2A, in airway smooth muscle. Knockdown of PP1 by lentivirus-mediated shRNA increased the acetylcholine-induced vimentin phosphorylation and smooth muscle contraction. Because vimentin phosphorylation is able to modulate p130 Crk-associated substrate (p130CAS) and actin polymerization, we also evaluated the role of PP1 in the biological processes. Silencing of PP1 also enhanced the agonist-induced the dissociation of p130CAS from vimentin and F/G-actin ratios (an index of actin polymerization). However, PP1 knockdown did not affect c-Abl tyrosine phosphorylation, an important molecule that controls actin dynamics. Taken together, these findings suggest that PP1 is a key protein serine/threonine phosphatase that controls vimentin Ser-56 dephosphorylation in smooth muscle. PP1 regulates actin polymerization by modulating the dissociation of p130CAS from vimentin, but not by affecting c-Abl tyrosine kinase.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 21 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 21 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 7 33%
Researcher 4 19%
Student > Doctoral Student 1 5%
Student > Bachelor 1 5%
Other 1 5%
Other 4 19%
Unknown 3 14%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 38%
Agricultural and Biological Sciences 5 24%
Computer Science 2 10%
Nursing and Health Professions 1 5%
Medicine and Dentistry 1 5%
Other 1 5%
Unknown 3 14%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. 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 25 July 2016.
All research outputs
#17,285,668
of 25,374,647 outputs
Outputs from Respiratory Research
#2,216
of 3,062 outputs
Outputs of similar age
#251,183
of 379,943 outputs
Outputs of similar age from Respiratory Research
#34
of 41 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 21st percentile – i.e., 21% of other outputs scored the same or lower than it.
So far Altmetric has tracked 3,062 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.9. This one is in the 18th percentile – i.e., 18% of its peers scored the same or lower than it.
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We're also able to compare this research output to 41 others from the same source and published within six weeks on either side of this one. This one is in the 2nd percentile – i.e., 2% of its contemporaries scored the same or lower than it.