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doi: 10.1242/10.1242/jcs.00131
Research Article |
1 European Molecular Biology Laboratory, Cell Biology Division, Heidelberg,
Germany
2 Institut Jacques Monod, Paris, France
3 Max-Planck-Institut für molekulare Physiologie, Department of Physical
Biochemistry, 44202 Dortmund, Germany
4 Potsdam University, Department of Cell Biology, Potsdam, Germany
5 King's College London, Muscle Cell Biology, The Randall Centre, New Hunt's
House, London SE1 1UL, UK
* Author for correspondence (e-mail: mathias.gautel{at}kcl.ac.uk)
Accepted 24 August 2002
Assembly of muscle sarcomeres is a complex dynamic process and involves a large number of proteins. A growing number of these have regulatory functions and are transiently present in the myofibril. We show here that the novel tubulin-associated RING/B-box protein MURF2 associates transiently with microtubules, myosin and titin during sarcomere assembly. During sarcomere assembly, MURF2 first associates with microtubules at the exclusion of tyrosinated tubulin. Then, MURF2-labelled microtubules associate transiently with sarcomeric myosin and later with A-band titin when non-striated myofibrils differentiate into mature sarcomeres. Finally, MURF2 labelled microtubules disappear from the sarcomere after the incorporation of myosin filaments and the elongation of titin. This suggests that the incorporation of myosin into nascent sarcomeres and the elongation of titin require an active, microtubule-dependent transport process and that MURF2-associated microtubules play a role in the alignment and extension of nascent sarcomeres. MURF2 is expressed in at least four isoforms, of which a 27 kDa isoform is cardiac specific. A C-terminal isoform is generated by alternative reading frame use, a novelty in muscle proteins. In mature cardiac sarcomeres, endogenous MURF2 can associate with the M-band, and is translocated to the nucleus. MURF2 can therefore act as a transient adaptor between microtubules, titin and nascent myosin filaments, as well as being involved in signalling from the sarcomere to the nucleus.
Key words: Myosin, Microtubules, Titin, MURF2, Myofibril assembly, Connectin
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