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First published online June 5, 2007

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MLP: on the shoulders of a giant

Muscle integrity relies upon interactions between sarcomeres (which contain the contractile actomyosin filaments and the giant protein titin) and the muscle cytoskeleton (which links the sarcomere to the cell membrane). On p. 2066, Kathleen Clark and colleagues reveal how muscle LIM protein (MLP), known to play crucial roles in cardiac muscle, underpins such interactions. They have generated flies in which the gene encoding MLP, Mlp84B, is mutated. The researchers find that larvae completely lacking Mlp84B have impaired muscle function and cannot pupate properly. They also observe that Mlp84B accumulates at the boundary of the Z-disc (the region where the actin and titin filaments originate) - and in particular colocalises with titin's N-terminus. Probing the interaction between Mlp84B and D-titin, the researchers find that flies lacking both Mlp84B and D-titin function suffer serious loss of muscle integrity. In humans, mutations in MLP are associated with cardiomyopathy and cardiac hypertrophy; these new insights into the way MLP functions in striated muscle could therefore help us understand this type of cardiac disease.

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Related articles in JCS:

The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity

Kathleen A. Clark, Jennifer M. Bland, and Mary C. Beckerle
JCS 2007 120: 2066-2077. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?