4.5 Article

Human α-synemin interacts directly with vinculin and metavinculin

Journal

BIOCHEMICAL JOURNAL
Volume 409, Issue -, Pages 657-667

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/BJ20071188

Keywords

costamere; focal adhesion; intermediate filament; metavinculin; synemin; vinculin

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Synemin is a very large, unique member of the IF (intermediate filament) protein superfamily. Association of synemin with the major IF proteins, desmin and/or vimentin, within muscle cells forms heteropolymeric IFs. We have previously identified interactions of avian synemin with a-actinin and vinculin. Avian synemin, however, is expressed as only one form, whereas human synemin is expressed as two major splice variants, namely alpha- and beta-synemins. The larger a-synemin contains an additional 312-amino-acid insert (termed SNTIII) located near the end of the long C-terminal tail domain. Whether alpha- and beta-synemins have different cellular functions is unclear. In the present study we show, by in vitro protein-protein interaction assays, that SNTIII interacts directly with both vinculin and metavinculin.

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