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  Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein

Pizon, V., Iakovenko, A., van der Ven, P. F. M., Kelly, R., Fatu, C., Fürst, D. O., et al. (2002). Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein. Journal of Cell Science, 115(23), 4469-4482. Retrieved from http://dx.doi.org/10.1242/jcs.00131.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0F36-C Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-0F37-A
Genre: Journal Article
Alternative Title : J. Cell Sci.

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 Creators:
Pizon, Véronique, Author
Iakovenko, Andrei1, Author
van der Ven, Peter F. M., Author
Kelly, Raymond1, Author
Fatu, Cristina1, Author
Fürst, Dieter O., Author
Karsenti, Eric, Author
Gautel, Mathias, Author
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              

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Free keywords: myosin; microtubules; titin; MURF2; myofibril; assembly; connectin
 Abstract: 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.

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Language(s): eng - English
 Dates: 2002
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 10854
URI: http://dx.doi.org/10.1242/jcs.00131
 Degree: -

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Title: Journal of Cell Science
  Alternative Title : J. Cell Sci.
Source Genre: Journal
 Creator(s):
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Publ. Info: -
Pages: - Volume / Issue: 115 (23) Sequence Number: - Start / End Page: 4469 - 4482 Identifier: -