Muscle length and myonuclear position are independently regulated by distinct Dynein pathways Journal Article
| Authors: | Folker, E. S.; Schulman, V. K.; Baylies, M. K. |
| Article Title: | Muscle length and myonuclear position are independently regulated by distinct Dynein pathways |
| Abstract: | Various muscle diseases present with aberrant muscle cell morphologies characterized by smaller myofibers with mispositioned nuclei. The mechanisms that normally control these processes, whether they are linked, and their contribution to muscle weakness in disease, are not known. We examined the role of Dynein and Dynein-interacting proteins during Drosophila muscle development and found that several factors, including Dynein heavy chain, Dynein light chain and Partner of inscuteable, contribute to the regulation of both muscle length and myonuclear positioning. However, Lis1 contributes only to Dynein-dependent muscle length determination, whereas CLIP-190 and Glued contribute only to Dynein-dependent myonuclear positioning. Mechanistically, microtubule density at muscle poles is decreased in CLIP-190 mutants, suggesting that microtubule-cortex interactions facilitate myonuclear positioning. In Lis1 mutants, Dynein hyperaccumulates at the muscle poles with a sharper localization pattern, suggesting that retrograde trafficking contributes to muscle length. Both Lis1 and CLIP-190 act downstream of Dynein accumulation at the cortex, suggesting that they specify Dynein function within a single location. Finally, defects in muscle length or myonuclear positioning correlate with impaired muscle function in vivo, suggesting that both processes are essential for muscle function. © 2012. Published by The Company of Biologists Ltd. |
| Keywords: | controlled study; unclassified drug; nonhuman; animals; animal tissue; gene; embryo; drosophila; morphology; regulatory mechanism; muscle weakness; cell nucleus; tubulin; microtubule; microtubules; drosophila proteins; developmental stage; bioaccumulation; mutant; muscles; dynein adenosine triphosphatase; muscle function; muscle cell; muscle development; microtubule-associated proteins; tropomyosin; guanine nucleotide dissociation inhibitors; dynein; muscle size; nuclear positioning; dynein heavy chain; dynein light chain; partner of inscuteable protein; protein clip 190; protein glued; protein lis1; clip 190 gene; lis1 gene; muscle length; dyneins |
| Journal Title: | Development |
| Volume: | 139 |
| Issue: | 20 |
| ISSN: | 0950-1991 |
| Publisher: | Company of Biologists |
| Date Published: | 2012-10-01 |
| Start Page: | 3827 |
| End Page: | 3837 |
| Language: | English |
| DOI: | 10.1242/dev.079178 |
| PROVIDER: | scopus |
| PUBMED: | 22951643 |
| PMCID: | PMC3445310 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 1 October 2012" - "CODEN: DEVPE" - "Source: Scopus" |
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