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        검색결과 3

        3.
        2004.12 KCI 등재 구독 인증기관 무료, 개인회원 유료
        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
        4,300원