Phosphatase Subfamily MTMR9

Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: Subfamily MTMR9

MTMR9 is a conserved pseudophosphatase across holozoan. It regulates active phosphatases of subfamily MTMR6.

Evolution

MTMR9 is found throughout holozoan. It is usually single copy per genome.

Domain Structure

MTMR9 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 MTMR subfamily, PH/GRAM domain can bind to phosphoinositide lipids. In Monosiga, the GRAM is replaced by a C1 domain, which is also a lipid-binding domain. Coiled-coil domain has been shown to mediate the interaction between MTMR9 and members of MTMR6 in human [1, 2, 3].

Catalytic activity and functions

MTMR9 is an inactive phosphatase (pseudophosphatase). MTMR9 binds to phosphatases of MTMR6 subfamilies: MTMR6 [2], MTMR7 [1], MTMR8 [3]. The interactions increase the enzymatic activity of these phosphatases. The interaction between MTMR9 and members of MTMR6 subfamily is also observed in C elegans [4].

References

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