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Sequences flanking the transmembrane segments facilitate mitochondrial localization and membrane fusion by mitofusin.
Huang, Xiaofang; Zhou, Xin; Hu, Xiaoyu; Joshi, Amit S; Guo, Xiangyang; Zhu, Yushan; Chen, Quan; Prinz, William A; Hu, Junjie.
Afiliação
  • Huang X; Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
  • Zhou X; Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China.
  • Hu X; Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
  • Joshi AS; Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China.
  • Guo X; Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
  • Zhu Y; Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China.
  • Chen Q; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
  • Prinz WA; Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
  • Hu J; Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China.
Proc Natl Acad Sci U S A ; 114(46): E9863-E9872, 2017 11 14.
Article em En | MEDLINE | ID: mdl-29093165
Mitochondria constantly divide and fuse. Homotypic fusion of the outer mitochondrial membranes requires the mitofusin (MFN) proteins, a family of dynamin-like GTPases. MFNs are anchored in the membrane by transmembrane (TM) segments, exposing both the N-terminal GTPase domain and the C-terminal tail (CT) to the cytosol. This arrangement is very similar to that of the atlastin (ATL) GTPases, which mediate fusion of endoplasmic reticulum (ER) membranes. We engineered various MFN-ATL chimeras to gain mechanistic insight into MFN-mediated fusion. When MFN1 is localized to the ER by TM swapping with ATL1, it functions in the maintenance of ER morphology and fusion. In addition, an amphipathic helix in the CT of MFN1 is exchangeable with that of ATL1 and critical for mitochondrial localization of MFN1. Furthermore, hydrophobic residues N-terminal to the TM segments of MFN1 play a role in membrane targeting but not fusion. Our findings provide important insight into MFN-mediated membrane fusion.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação ao GTP / Proteínas de Transporte da Membrana Mitocondrial / Fusão de Membrana / Proteínas de Membrana / Mitocôndrias Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2017 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação ao GTP / Proteínas de Transporte da Membrana Mitocondrial / Fusão de Membrana / Proteínas de Membrana / Mitocôndrias Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2017 Tipo de documento: Article País de afiliação: China