Colocation of Tpm3.1 and myosin IIa heads defines a discrete subdomain in stress fibres.


Journal

Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457

Informations de publication

Date de publication:
08 08 2019
Historique:
received: 13 12 2018
accepted: 06 07 2019
pubmed: 25 7 2019
medline: 10 7 2020
entrez: 24 7 2019
Statut: epublish

Résumé

Co-polymers of tropomyosin and actin make up a major fraction of the actin cytoskeleton. Tropomyosin isoforms determine the function of an actin filament by selectively enhancing or inhibiting the association of other actin binding proteins, altering the stability of an actin filament and regulating myosin activity in an isoform-specific manner. Previous work has implicated specific roles for at least five different tropomyosin isoforms in stress fibres, as depletion of any of these five isoforms results in a loss of stress fibres. Despite this, most models of stress fibres continue to exclude tropomyosins. In this study, we investigate tropomyosin organisation in stress fibres by using super-resolution light microscopy and electron microscopy with genetically tagged, endogenous tropomyosin. We show that tropomyosin isoforms are organised in subdomains within the overall domain of stress fibres. The isoforms Tpm3.1 and 3.2 (hereafter Tpm3.1/3.2, encoded by

Identifiants

pubmed: 31331962
pii: jcs.228916
doi: 10.1242/jcs.228916
pii:
doi:

Substances chimiques

Protein Isoforms 0
TPM3 protein, human 0
Tropomyosin 0
Nonmuscle Myosin Type IIA EC 3.6.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2019. Published by The Company of Biologists Ltd.

Déclaration de conflit d'intérêts

Competing interestsE.C.H. and P.W.G. are directors and shareholders in TroBio Therapeutics, a company that is commercialising anti-tropomyosin drugs for the treatment of cancer and their labs receive funding from TroBio to evaluate anti-tropomyosin drug candidates. J.C.M.M., N.S.B., M.L.C., A.B., R.M.W., N.A. and R.G.P. have no competing interests.

Auteurs

Joyce C M Meiring (JCM)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Nicole S Bryce (NS)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Maria Lastra Cagigas (M)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Aleš Benda (A)

Biomedical Imaging Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.

Renee M Whan (RM)

Biomedical Imaging Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.

Nicholas Ariotti (N)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.
Electron Microscope Unit, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.

Robert G Parton (RG)

Cell Biology and Molecular Medicine Division, Institute for Molecular Bioscience, University of Queensland, St Lucia, QLD 4072, Australia.
Centre for Microscopy and Microanalysis, University of Queensland, St Lucia, QLD 4072, Australia.

Jeffrey H Stear (JH)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Edna C Hardeman (EC)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Peter W Gunning (PW)

School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia p.gunning@unsw.edu.au.

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Classifications MeSH