Difference between revisions of "Phosphatase Subfamily MTMR5"
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===Catalytic activity and functions=== | ===Catalytic activity and functions=== | ||
| − | + | MTMR5 subfamily is conservatively inactive in metazoan. Human MTMR5 interact with MTMR2 (see [[Phosphatase_Subfamily_MTMR1|MTMR1 subfamily]]) via its coiled-coil domain and mutations in the coiled-coil domain of either MTMR2 or MTMR5 abrogate this interaction. Through this interaction, MTMR5 increases the enzymatic activity of MTMR2 and dictates its subcellular localization <cite>kim03</cite>. | |
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===References=== | ===References=== | ||
Revision as of 23:50, 30 December 2014
Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: Subfamily MTMR5 (SBF)
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Evolution
MTMR5 subfamily is found throughout metazoan. It consists of two members in human, MTMR5 and MTMR13, also called SBF1 and SBF2, respectively. In fruit fly and C elegans, a single copy is found.
Domain Structure
MTMR5 subfamily has a DENN domain, PH/GRAM domain, phosphatase domain, coiled-coil domain and PH domain. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins.
Catalytic activity and functions
MTMR5 subfamily is conservatively inactive in metazoan. Human MTMR5 interact with MTMR2 (see MTMR1 subfamily) via its coiled-coil domain and mutations in the coiled-coil domain of either MTMR2 or MTMR5 abrogate this interaction. Through this interaction, MTMR5 increases the enzymatic activity of MTMR2 and dictates its subcellular localization [1].
References
- Blondeau F, Laporte J, Bodin S, Superti-Furga G, Payrastre B, and Mandel JL. Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. Hum Mol Genet. 2000 Sep 22;9(15):2223-9. DOI:10.1093/oxfordjournals.hmg.a018913 |
