Difference between revisions of "Phosphatase Subfamily MTMR3"

Revision as of 20:02, 30 December 2014

Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin: MTMR3

MTMR1 is a lipid phosphatase that dephosphorylates the second messenger phosphatidylinositol 3-monophosphate [PI(3)P].

Evolution

MTMR1 is in metazoan. It consists of two members in human, MTMR3 and MTMR4. In fruit fly and C elegans, a single copy is found.

Domain Structure

MTMR3 subfamily has a conserved domain combination: a divergent PH/GRAM domain, an active phosphatase domain and an atypical FYVE domain. It has been shown that the FYVE domain of MTMR3 is atypical in that it neither confers endosomal localisation nor binds to the lipid PtdIns3P. Furthermore it is not required for in vitro enzyme activity of MTMR3. In contrast, the PH/GRAM domain is able to bind to phosphoinositide lipids [1].

Catalytic activity and functions

Human MTMR3 is an inositol lipid 3-phosphatase, with a so-far-unique substrate specificity. It is able to hydrolyze PtdIns3P and PtdIns(3,5)P2, both in vitro and when heterologously expressed in S. cerevisiae. Thus, MTMR3 plays critical role in the cellular production of PtdIns5P [2].

Related Kinases

See PI3K.

References

1. Lorenzo O, Urbé S, and Clague MJ. Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3. J Cell Sci. 2005 May 1;118(Pt 9):2005-12. DOI:10.1242/jcs.02325 | PubMed ID:15840652 | HubMed [Lorenzo05]
2. Walker DM, Urbé S, Dove SK, Tenza D, Raposo G, and Clague MJ. Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr Biol. 2001 Oct 16;11(20):1600-5. DOI:10.1016/s0960-9822(01)00501-2 | PubMed ID:11676921 | HubMed [walker01]
3. Zhao R, Qi Y, Chen J, and Zhao ZJ. FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate. Exp Cell Res. 2001 May 1;265(2):329-38. DOI:10.1006/excr.2001.5185 | PubMed ID:11302699 | HubMed [zhao01]