Ontology highlight
ABSTRACT:
SUBMITTER: Ma J
PROVIDER: S-EPMC2562989 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
Ma Junfeng J Zeng Fenghua F Ho Wanting Tina WT Teng Lirong L Li Qingshan Q Fu Xueqi X Zhao Zhizhuang Joe ZJ
Journal of cellular biochemistry 20080801 5
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 reveale ...[more]