作者: Matthew W. Kemp , Ben Edwards , Matthew Burgess , W. Thomas Clarke , George Nicholson
DOI: 10.1016/J.JSB.2008.11.002
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摘要: Abstract Syncoilin is a 64 kDa intermediate filament (IF) protein expressed in myocytes at the sarcolemma, perinucleus, myotendenous and neuromuscular junctions. Here we present revised domain projection structural analysis for original isoform (sync-1) introduce two novel syncoilin isoforms (sync-2 sync-3) generated by exon splicing. On basis of consensus identity propose that be reclassified as type III IF protein. All three lack L1 domain, significant departure from standard rod projections likely to impact significantly on their biological function. Our analyses indicate unlikely form classical structures itself, difference C-terminal structure between indicates they may play divergent roles myocytes. We show despite lacking an apparent role striated muscle, are differentially strongly upregulated response cardiotoxin induced regeneration denervation atrophy C57BL/6 mouse, possibly suggesting atypical muscle.