Difference between revisions of "Phosphatase Subfamily MTMR6"
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===Catalytic activity and functions=== | ===Catalytic activity and functions=== | ||
| − | The enzymatic activity of all three human MTMR6s are up-regulated by pseudophosphatase MTMR9 through protein interactions<cite>zou09, Mochizuki03, zou12</cite>. The interaction between MTMR9 and MTMR6 subfamily is also observed in C elegans <cite>marie10</cite>. | + | The enzymatic activity of all three human MTMR6s are up-regulated by pseudophosphatase MTMR9 through protein interactions <cite>zou09, Mochizuki03, zou12</cite>. The interaction between MTMR9 and MTMR6 subfamily is also observed in C elegans <cite>marie10</cite>. |
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| + | Though all of MTMR6, MTMR7 and MTMR8 are 3-phosphatase, they have different preferences of substrates. MTMR6/R9 complex that regulates PtdIns (3, 5)P2 levels and thereby affects apoptosis; MTMR8/R9 complex down-regulates the levels of PthIns(3)P and blocks the autophagic process <cite>zou09, zou12</cite>; MTMR7/MTMR9 dephosphorylates phosphatidylinositol 3-phosphate and Ins(1,3)P2 in neuronal cells <cite>Mochizuki03</cite>. | ||
===References=== | ===References=== | ||
Revision as of 19:31, 31 December 2014
Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: Subfamily MTMR6
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Evolution
MTMR6 subfamily is found throughout holozoan. Human and most if not all vertebrates has three members per genome: MTMR6, MTMR7 and MTMR8. Other metazoan such as fruit fly and C elegans has a single member.
Domain Structure
MTMR6 subfamily has three domains: PH/GRAM, phosphatase domain and coiled-coil domain. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins. As shown in MTMR3 subfamily, PH/GRAM domain can bind to phosphoinositide lipids. Coiled-coil domain has been shown to mediate the interaction with MTMR9 in human [1, 2, 3].
Catalytic activity and functions
The enzymatic activity of all three human MTMR6s are up-regulated by pseudophosphatase MTMR9 through protein interactions [1, 2, 3]. The interaction between MTMR9 and MTMR6 subfamily is also observed in C elegans [4].
Though all of MTMR6, MTMR7 and MTMR8 are 3-phosphatase, they have different preferences of substrates. MTMR6/R9 complex that regulates PtdIns (3, 5)P2 levels and thereby affects apoptosis; MTMR8/R9 complex down-regulates the levels of PthIns(3)P and blocks the autophagic process [2, 3]; MTMR7/MTMR9 dephosphorylates phosphatidylinositol 3-phosphate and Ins(1,3)P2 in neuronal cells [1].
References
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