期刊
JOURNAL OF CELLULAR BIOCHEMISTRY
卷 104, 期 5, 页码 1843-1852出版社
WILEY
DOI: 10.1002/jcb.21752
关键词
tyrosine phosphatase; myotubularin; phosphoinositide; aging; locomotion
资金
- NHLBI NIH HHS [R01 HL079441, R01 HL079441-02, R01 HL076309-05, HL076309, HL079441, R01 HL076309] Funding Source: Medline
The myotubularin (MTM) enzymes are phosphatidylinositol 3-phosphate(PI3P) and phosphatidylinositol 3,5-bisphosphate phosphatases. Mutation of MTM1, the founder member of this family, is responsible for X-linked myotubular myopathy in humans. Here, we have isolated and characterized a Caenorhabditis elegans homology of the enzymes designated ceMTM3. ceMTM3 preferably dephosphorylates PI3P and contains a FYVE lipid-binding domain at its C-terminus which binds PI3P. Immunoblotting analyses revealed that the enzyme is expressed during the early development and adulthood of the animal. Immunofluorescent staining revealed predominant expression of the enzyme in eggs and muscles. Knockdown of the enzyme by using feeding-based RNA interference resulted in an increased level of PI3P and caused severe impairment of body movement of the worms at their post-reproductive ages and significantly shortened their lifespan. This study thus reveals an important role of the MTM phosphatases in maintaining muscle function, which may have clinical implications in prevention and treatment of sarcopenia.
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