The myotubularin (MTM) family constitutes one of the most highly conserved protein-tyrosine phosphatase subfamilies in eukaryotes. MTM1, the archetypal member of this family, is mutated in X-l띠ked myotubular myopathy, whereas mutations in the MTM related (MTMR)2 gene cause the type 4B Charcot-Marie-Tooth disease, a severe hereditary motor and sensory neuropathy. In this study, we investigated the role of pleckstrin homology (PH) domain of MTMR2. We demonstrate here that the PH domain of MTMR2 directly interacts with phosphatidylinositol (PtdIns)(3)P, PtdIns(5)P, and to a Iesser extent Pt，이 ns(4)P. Furthermore, MTMR2-PH domain is required for targe띠g Mη00 to the 다πoplasmic compartment. Mutation in the PH domain abolished its phospholipid binding ability and MTMR2 subcel1ular localization. These results su잃.est that the PH domain regulates MTMR2 1αalization and function through its interaction with phosphoinosi디des and give us the clue to understand the pathogenic effect of PH domain

• Soo A Kim(Depatment of Ora1 Pathology, BK 21 Project，School of DentistJy, Chosun University) | 김수아
• Won Hak Lee(Depatment of Ora1 Pathology, BK 21 Project，School of DentistJy, Chosun University) | 이원학
• Sang Gun Ahn(Depatment of Ora1 Pathology, BK 21 Project，School of DentistJy, Chosun University) | 안상건
• Jung Hoon Yoon(Depatment of Ora1 Pathology, BK 21 Project，School of DentistJy, Chosun University) | 윤정훈