Biochemical and Biophysical Research Communications
Regular ArticleSynemin Contains the Rod Domain of Intermediate Filaments
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The cytoskeleton and connected elements in bone cell mechano-transduction
2021, BoneCitation Excerpt :Global deletion of synemin results in osteopenia in male mice, with decreased trabecular bone, reduced cross-sectional thickness, and decreased osteoblast number despite an increased osteogenic capacity [172]. Unlike most intermediate filaments, synemin does not homopolymerize [176] or form 1:1 heteropolymers with other subunits. Rather, it co-assembles into desmin or vimentin filaments [177–179] and associates with keratin filaments [178] as well as with other proteins [180].
Absence of synemin in mice causes structural and functional abnormalities in heart
2018, Journal of Molecular and Cellular CardiologyCitation Excerpt :Here we focus on synemin and its role in the heart. Synemin is a large IF protein that can be expressed in one of two isoforms, α (~ 210 kDa), and β (~ 180 kDa) [17,18]. Unlike desmin, and keratins 8 and 18, and 8 and 19, synemin is incapable of forming stable IFs on its own and thus requires other IF proteins to form heterofilaments [19].
Synemin Molecular Features and the Use of Proximity Ligation Assay to Study Its Interactions
2016, Methods in EnzymologyCitation Excerpt :These early results suggested that synemin was an IF-associated protein rather than an IF protein and accordingly coined the name from the Greek syn (with) and nema (filament) (Granger & Lazarides, 1980). Sequencing of avian (Becker, Bellin, Sernett, Huiatt, & Robson, 1995; Bellin et al., 1999) and mammalian (Mizuno, Thompson, et al., 2001; Titeux et al., 2001; Xue et al., 2004) synemin cDNAs revealed, however, that synemin is a bona fide IF protein since it possesses structural features common to all IF proteins, i.e., a central α-helical domain of 310 amino acids interrupted at specific positions by short non-α-helical regions (linkers). Synemin sequence shares the most similarity with nestin providing the rationale to group these two proteins into a class VI IF proteins (Guérette, Khan, Savard, & Vincent, 2007).
α-Synemin localizes to the M-band of the sarcomere through interaction with the M10 region of titin
2014, FEBS LettersCitation Excerpt :This same fragment bound to vinculin in blot overlay assays and also co-localized with vinculin in cultured cells emphasizing its importance in protein–protein interaction [10]. The fact that synemin is a structural IF protein and an AKAP is already known [1,36]; however the individual role of each isoform is less established. As discussed earlier, functional differences between the isoforms are likely based on different subcellular locations and/or binding proteins.
Synemin down-regulation in human hepatocellular carcinoma does not destabilize cytoskeletons in vivo
2011, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The mechanism of synemin knock-down action on the liver cell transformation is still unclear. Although synemin was initially classified as an IFAP [10]; subsequent study discovered that it is not an IFAP, but instead contains the characteristic IF rod domain and is a novel member of the IF protein superfamily [29]. Recently synemin was identified in association with desmin- and/or vimentin and functions as a component of heteropolymeric IFs [12].
Synemin interacts with the LIM domain protein zyxin and is essential for cell adhesion and migration
2010, Experimental Cell Research