Difference between revisions of "Phosphatase Subfamily MTMR6"
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===Domain Structure=== | ===Domain Structure=== | ||
| − | MTMR6 subfamily has three domains: [http://pfam.xfam.org/family/PF02893.15 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 [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], PH/GRAM domain can bind to phosphoinositide lipids. | + | MTMR6 subfamily has three domains: [http://pfam.xfam.org/family/PF02893.15 PH/GRAM], phosphatase domain and coiled-coil domain. Coiled-coil domain has been shown to mediate the interaction with [[Phosphatase_Subfamily_MTMR9|MTMR9]] in human <cite>Mochizuki03, zou09, zou12</cite>. The GRAM domain is similar to PH domain in structure and is found in membrane-associated proteins. As shown in [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], PH/GRAM domain can bind to phosphoinositide lipids. But, in the case of human MTMR6, small GTPase Rab1B interacts with MTMR6 via PH/GRAM domain, and therefore regulates cellular localization in the early secretory and autophagic pathways <cite>Mochizuki13</cite>. |
===Catalytic activity and functions=== | ===Catalytic activity and functions=== | ||
Revision as of 19:45, 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. Coiled-coil domain has been shown to mediate the interaction with MTMR9 in human [1, 2, 3]. 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. But, in the case of human MTMR6, small GTPase Rab1B interacts with MTMR6 via PH/GRAM domain, and therefore regulates cellular localization in the early secretory and autophagic pathways [4].
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 [5].
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].
MTMR7 has also been reported to regulate T-cell differentiation and Protein kinase B AKT signaling, possibly through regulation of phosphatidylinositol [3,4,5]-trisphosphate activity [6].
References
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