Ontology highlight
ABSTRACT:
SUBMITTER: Gokhin DS
PROVIDER: S-EPMC4689220 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Gokhin David S DS Ochala Julien J Domenighetti Andrea A AA Fowler Velia M VM
Development (Cambridge, England) 20151119 24
The sarcomeric tropomodulin (Tmod) isoforms Tmod1 and Tmod4 cap thin filament pointed ends and functionally interact with the leiomodin (Lmod) isoforms Lmod2 and Lmod3 to control myofibril organization, thin filament lengths, and actomyosin crossbridge formation in skeletal muscle fibers. Here, we show that Tmod4 is more abundant than Tmod1 at both the transcript and protein level in a variety of muscle types, but the relative abundances of sarcomeric Tmods are muscle specific. We then generate ...[more]