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Compartment-alizing metabolic enzymes in muscle

In skeletal and cardiac muscle, metabolic enzymes reside in specific regions of the sarcomere (in the I-band and the M-band). This appears to allow them to generate high concentrations of ATP where it is needed for muscle contraction. How the enzymes are targeted to these locations has remained a mystery, but Jean-Clause Perriard and co-workers now implicate two proteins in this process: the LIM-domain protein DRAL/FHL-2 and titin — the `sarcomeric ruler' molecule that forms an elastic scaffold spanning half a sarcomere (see p. 4925). Combining two-hybrid assays, colocalization and pull-down experiments, they show that DRAL/FHL-2, a heart-specific LIM-only protein, binds to two sites in the giant titin molecule: one in the heart-specific insertion N2B, which is positioned in the I-band; the other in insertion sequence 2 (is2), which is positioned in the M-band. The authors demonstrate that creatine kinase, adenylate kinase and phosphofructokinase also bind to DRAL/FHL-2. They therefore propose that DRAL/FHL-2 acts as an adaptor that recruits these metabolic enzymes to titin-defined sites in the cardiac sarcomere.

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Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2

Stephan Lange, Daniel Auerbach, Patricia McLoughlin, Evelyne Perriard, Beat W. Schäfer, Jean-Claude Perriard, and Elisabeth Ehler
JCS 2002 115: 4925-4936. [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?