Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C.

Mutations in the genes encoding the inner nuclear membrane proteins lamin A/C and emerin produce cardiomyopathy and muscular dystrophy in humans and mice. The mechanism by which these broadly expressed gene products result in tissue-specific dysfunction is not known. We have identified a protein of the inner nuclear membrane that ...
is highly expressed in striated and smooth muscle. This protein, myne-1 (myocyte nuclear envelope), is predicted to have seven spectrin repeats, an interrupted LEM domain and a single transmembrane domain at its C-terminus. We found that myne-1 is expressed upon early muscle differentiation in multiple intranuclear foci concomitant with lamin A/C expression. In mature muscle, myne-1 and lamin A/C are perfectly colocalized, although colocalization with emerin is only partial. Moreover, we show that myne-1 and lamin A/C coimmunoprecipitate from differentiated muscle in vitro. The muscle-specific inner nuclear envelope expression of myne-1, along with its interaction with lamin A/C, indicates that this gene is a potential mediator of cardiomyopathy and muscular dystrophy.
Mesh Terms:
Amino Acid Sequence, Animals, Cell Differentiation, Cell Line, Fluorescent Antibody Technique, Immunohistochemistry, Laminin, Membrane Proteins, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Muscle Proteins, Muscle, Skeletal, Myocardium, Nerve Tissue Proteins, Nuclear Envelope, Nuclear Proteins, Protein Structure, Secondary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid, Sequence Homology, Amino Acid, Spectrin, Subcellular Fractions
J. Cell. Sci.
Date: Jan. 01, 2002
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