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Gene Review:

MTMR3 - myotubularin related protein 3

Homo sapiens

Synonyms: FYVE domain-containing dual specificity protein phosphatase 1, FYVE-DSP1, KIAA0371, Myotubularin-related protein 3, Phosphatidylinositol-3,5-bisphosphate 3-phosphatase, ...

Zhao, R. et al., Taylor, G.S. et al., Yoo, Y.D. et al., Schaletzky, J. et al., Zhao, R. et al., et al.

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Disease relevance of MTMR3

Herein, we report that the human myotubularin-related protein (KIAA0371) induced growth suppression of lung cancer cells [1].

High impact information on MTMR3

Both the recombinant yeast enzyme and a human myotubularin-related protein (KIAA0371) are able to dephosphorylate PI(3)P in vitro, suggesting that this activity is intrinsic to all myotubularin family members [2].
MTM1 is a phosphatidylinositol phosphatase with reported specificity toward PtdIns3P, while the related proteins MTMR2 and MTMR3 hydrolyze both PtdIns3P and PtdIns(3,5)P2 [3].
We also report the capacity of several family members to self-associate, including MTMR3 and MTMR4 [4].
Sequence alignment revealed that the catalytic phosphatase domain of FYVE-DSP1 closely resembled that of myotubularin, while its FYVE domain has all the conserved amino acid residues found in other proteins of the same family [5].
FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain [5].

Analytical, diagnostic and therapeutic context of MTMR3

Genomic sequence analyses revealed that the FYVE-DSP1 and FYVE-DSP2 genes share similar intron/exon organization [6].
Finally, PCR analyses demonstrated that FYVE-DSP1 is widely distributed in human tissues but different spliced forms expressed differently [5].

References

The human myotubularin-related protein suppresses the growth of lung carcinoma cells. Yoo, Y.D., Cho, S.M., Kim, J.S., Chang, Y.S., Ahn, C.M., Kim, H.J. Oncol. Rep. (2004) [Pubmed]
Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. Taylor, G.S., Maehama, T., Dixon, J.E. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases. Schaletzky, J., Dove, S.K., Short, B., Lorenzo, O., Clague, M.J., Barr, F.A. Curr. Biol. (2003) [Pubmed]
Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosomerelated functions. Lorenzo, O., Urbé, S., Clague, M.J. J. Cell. Sci. (2006) [Pubmed]
FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain. Zhao, R., Qi, Y., Zhao, Z.J. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate. Zhao, R., Qi, Y., Chen, J., Zhao, Z.J. Exp. Cell Res. (2001) [Pubmed]

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