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Updated: Jul 4, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Nuclear localization of Myomesin-1: possible functions
Kumar B Reddy1, Joan E B Fox, Maureen G Price
1Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue #NB5, Cleveland, OH 44195, USA. reddyk@ccf.org
Abstract:
Myomesin-I (also known as Skelemin) is a approximately 185 kDa protein, which is highly expressed in striated muscle. It contains the prototypic class-I (type-III fibronectin) and class-II (C2-immunoglobulin) motifs. Previous studies have shown the presence of Myomesin-I at the M-line of the sarcomere, where it is thought to interact with thick filament constituents. As reported previously, Myomesin-I was localized to the M-line in the adult cardiac myocytes (adult-myocytes). However, we found that Myomesin-I was also present exclusively in the nucleus of myocytes isolated from new born pups (neonatal-myocytes). In addition, the ectopically expressed Myomesin-I was primarily targeted to the nucleus, similar to the neonatal myocytes. Further investigations revealed that the nuclear-targeting signals were present within the N-terminal 256 residues. A strong consensus sequence for sumoylation is present within the N-terminal 256 residues and is implicated in the shuttling of Myomesin-I between nucleus and cytoplasm. Gene array analysis showed that the presence of Myomesin-I in the nucleus led to the differential expression of more than 42 genes. These studies show a novel and previously unknown localization and function for Myomesin-I.
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