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Alteration of Tropomyosin-binding Properties of Tropomodulin-1 Affects Its Capping Ability and Localization in Skeletal Myocytes*

Overview of attention for article published in Journal of Biological Chemistry, December 2012
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Article details
Title
Alteration of Tropomyosin-binding Properties of Tropomodulin-1 Affects Its Capping Ability and Localization in Skeletal Myocytes*
Published in
Journal of Biological Chemistry, December 2012
DOI 10.1074/jbc.m112.434522
Pubmed ID
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Abstract

Tropomodulin (Tmod) is an actin-capping protein that binds to the two tropomyosins (TM) at the pointed end of the actin filament to prevent further actin polymerization and depolymerization. Therefore, understanding the role of Tmod is very important when studying actin filament dependent processes such as muscle contraction and intracellular transport. The capping ability of Tmod is highly influenced by TM and is 1000-fold greater in the presence of TM. There are four Tmod isoforms (Tmod1-4), three of which, Tmod1, Tmod3, and Tmod4, are expressed in skeletal muscles. The affinity of Tmod1 to skeletal striated TM (stTM) is higher than that of Tmod3 and Tmod4 to stTM. In this study, we tested mutations in the TM-binding sites of Tmod1, using circular dichroism (CD) and prediction analysis (PONDR). The mutations R11K, D12N, and Q144K were chosen because they decreased the affinity of Tmod1 to stTM, making it similar to that of affinity of Tmod3 and Tmod4 to stTM. Significant reduction of inhibition of actin pointed-end polymerization in the presence of stTM was shown for Tmod1 (R11K/D12N/Q144K) as compared with WT Tmod1. When GFP-Tmod1 and mutants were expressed in primary chicken skeletal myocytes, decreased assembly of Tmod1 mutants was revealed. This indicates a direct correlation between TM-binding and the actin-capping abilities of Tmod. Our data confirmed the hypothesis that assembly of Tmod at the pointed-end of the actin filament depends on its TM-binding affinity.

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Geographical breakdown

Geographical breakdown
Country Count As %
Unknown 9 100%

Demographic breakdown

Readers by professional status
Readers by professional status Count As %
Researcher 3 33%
Student > Master 2 22%
Student > Ph. D. Student 1 11%
Professor > Associate Professor 1 11%
Unknown 2 22%
Readers by discipline
Readers by discipline Count As %
Agricultural and Biological Sciences 5 56%
Biochemistry, Genetics and Molecular Biology 1 11%
Engineering 1 11%
Unknown 2 22%
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 02 January 2013.
All research outputs
#22,759,802
of 25,374,917 outputs
Outputs from Journal of Biological Chemistry
#82,452
of 85,240 outputs
Outputs of similar age
#258,365
of 288,792 outputs
Outputs of similar age from Journal of Biological Chemistry
#412
of 551 outputs
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So far Altmetric has tracked 85,240 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.1. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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