Nuclear localization of Myomesin-1: possible functions.

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.

authors

Reddy KB,Fox JE,Price MG,Kulkarni S,Gupta S,Das B,Smith DM

doi

10.1007/s10974-008-9137-x

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

1-8

issue

1

eissn

0142-4319

issn

1573-2657

journal_volume

29

pub_type

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