Recruitment Kinetics of Tropomyosin Tpm3.1 to Actin Filament Bundles in the Cytoskeleton Is Independent of Actin Filament Kinetics
Publication Date
December 15, 2016
Authors
Mark A. Appaduray, Andrius Masedunskas, Nicole S. Bryce, Christine A. Lucas, et al
Volume
11
Issue
12
Pages
e0168203
DOI
https://dx.plos.org/10.1371/journal.pone.0168203
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0168203
Scopus
85006421883
Mendeley
http://www.mendeley.com/research/recruitment-kinetics-tropomyosin-tpm31-actin-filament-bundles-cytoskeleton-independent-actin-filamen
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Mendeley | Further Information

{"title"=>"Recruitment kinetics of tropomyosin tpm3.1 to actin filament bundles in the cytoskeleton is independent of actin filament kinetics", "type"=>"journal", "authors"=>[{"first_name"=>"Mark A.", "last_name"=>"Appaduray", "scopus_author_id"=>"57076880000"}, {"first_name"=>"Andrius", "last_name"=>"Masedunskas", "scopus_author_id"=>"24071274000"}, {"first_name"=>"Nicole S.", "last_name"=>"Bryce", "scopus_author_id"=>"6506159308"}, {"first_name"=>"Christine A.", "last_name"=>"Lucas", "scopus_author_id"=>"56608661100"}, {"first_name"=>"Sean C.", "last_name"=>"Warren", "scopus_author_id"=>"55481468100"}, {"first_name"=>"Paul", "last_name"=>"Timpson", "scopus_author_id"=>"8340574400"}, {"first_name"=>"Jeffrey H.", "last_name"=>"Stear", "scopus_author_id"=>"6603304234"}, {"first_name"=>"Peter W.", "last_name"=>"Gunning", "scopus_author_id"=>"26643395700"}, {"first_name"=>"Edna C.", "last_name"=>"Hardeman", "scopus_author_id"=>"35512397100"}], "year"=>2016, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pui"=>"613688020", "doi"=>"10.1371/journal.pone.0168203", "sgr"=>"85006421883", "scopus"=>"2-s2.0-85006421883", "pmid"=>"27977753"}, "id"=>"2dfad620-97f3-3656-8f64-73e00cb6f315", "abstract"=>"The actin cytoskeleton is a dynamic network of filaments that is involved in virtually every cellular process. Most actin filaments in metazoa exist as a co-polymer of actin and tropomyosin (Tpm) and the function of an actin filament is primarily defined by the specific Tpm isoform associated with it. However, there is little information on the interdependence of these co-polymers during filament assembly and disassembly. We addressed this by investigating the recovery kinetics of fluorescently tagged isoform Tpm3.1 into actin filament bundles using FRAP analysis in cell culture and in vivo in rats using intracellular intravital microscopy, in the presence or absence of the actin-targeting drug jasplakinolide. The mobile fraction of Tpm3.1 is between 50% and 70% depending on whether the tag is at the C- or N-terminus and whether the analysis is in vivo or in cultured cells. We find that the continuous dynamic exchange of Tpm3.1 is not significantly impacted by jasplakinolide, unlike tagged actin. We conclude that tagged Tpm3.1 may be able to undergo exchange in actin filament bundles largely independent of the assembly and turnover of actin.", "link"=>"http://www.mendeley.com/research/recruitment-kinetics-tropomyosin-tpm31-actin-filament-bundles-cytoskeleton-independent-actin-filamen", "reader_count"=>9, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Researcher"=>1, "Student > Ph. D. Student"=>2, "Student > Bachelor"=>3, "Lecturer"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Researcher"=>1, "Student > Ph. D. Student"=>2, "Student > Bachelor"=>3, "Lecturer"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Agricultural and Biological Sciences"=>5, "Physics and Astronomy"=>1, "Biochemistry, Genetics and Molecular Biology"=>1}, "reader_count_by_subdiscipline"=>{"Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>5}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"United Kingdom"=>1}, "group_count"=>0}

Scopus | Further Information

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