MG53 Regulates Membrane Budding and Exocytosis in Muscle Cells

被引:100
作者
Cai, Chuanxi [2 ]
Masumiya, Haruko [1 ]
Weisleder, Noah [2 ]
Pan, Zui [2 ]
Nishi, Miyuki [1 ,4 ]
Komazaki, Shinji [5 ]
Takeshima, Hiroshi [1 ,4 ]
Ma, Jianjie [2 ,3 ]
机构
[1] Tohoku Univ, Grad Sch Med, Dept Med Chem, Sendai, Miyagi 9808575, Japan
[2] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Physiol & Biophys, Piscataway, NJ 08854 USA
[3] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Med, Piscataway, NJ 08854 USA
[4] Kyoto Univ, Grad Sch Pharmaceut Sci, Dept Biol Chem, Kyoto 6068501, Japan
[5] Saitama Med Univ, Dept Anat, Saitama 3500495, Japan
基金
美国国家卫生研究院;
关键词
DUCHENNE-MUSCULAR-DYSTROPHY; RING-FINGER PROTEIN; SKELETAL-MUSCLE; RYANODINE RECEPTORS; MONKEY TRIM5-ALPHA; SARCOPLASMIC-RETICULUM; TRIAD JUNCTION; CAVEOLIN-3; RESTRICTION; DOMAINS;
D O I
10.1074/jbc.M808866200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Membrane recycling and remodeling contribute to multiple cellular functions, including cell fusion events during myogenesis. We have identified a tripartite motif (TRIM72) family member protein named MG53 and defined its role in mediating the dynamic process of membrane fusion and exocytosis in striated muscle. MG53 is a muscle-specific protein that contains a TRIM motif at the amino terminus and a SPRY motif at the carboxyl terminus. Live cell imaging of green fluorescent protein-MG53 fusion construct in cultured myoblasts showed that although MG53 contains no trans-membrane segment it is tightly associated with intracellular vesicles and sarcolemmal membrane. RNA interference-mediated knockdown of MG53 expression impeded myoblast differentiation, whereas overexpression of MG53 enhanced vesicle trafficking to and budding from sarcolemmal membrane. Co-expression studies indicated that MG53 activity is regulated by a functional interaction with caveolin-3. Our data reveal a new function for TRIM family proteins in regulating membrane trafficking and fusion in striated muscles.
引用
收藏
页码:3314 / 3322
页数:9
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