Difference between revisions of "Phosphatase Subfamily MTMR6"

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(Catalytic activity and functions)
(Catalytic activity and functions)
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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>.
 
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>.
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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 <cite>guo13</cite>.
  
 
===References===
 
===References===

Revision as of 19:38, 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].

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 [5].

References

Error fetching PMID 12890864:
Error fetching PMID 19038970:
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Error fetching PMID 21076391:
  1. Error fetching PMID 12890864: [Mochizuki03]
  2. Error fetching PMID 19038970: [zou09]
  3. Error fetching PMID 22647598: [zou12]
  4. Error fetching PMID 21076391: [marie10]
All Medline abstracts: PubMed | HubMed