Junjie Hu
Institute of Biophysics
Chinese Academy of Sciences
China
Biography
Education and Training 2000, B.S. Biochemistry, Fudan University, Shanghai, China 2005, Ph.D., Biomedical Science, New York University 2008, Cell Biology, Postdoctoral, Harvard Medical School/HHMI Positions and Employment 2013-present Professor, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 2008-2012   Professor, Department of Genetics and Cell Biology, College of Life Sciences,Nankai University, Tianjin, China Honors 2012 HHMI International Early Career Scientist Education and Training 2000, B.S. Biochemistry, Fudan University, Shanghai, China 2005, Ph.D., Biomedical Science, New York University 2008, Cell Biology, Postdoctoral, Harvard Medical School/HHMI Positions and Employment 2013-present Professor, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences 2008-2012   Professor, Department of Genetics and Cell Biology, College of Life Sciences,Nankai University, Tianjin, China Honors 2012 HHMI International Early Career Scientist
Research Interest
Biological membranes adopt different shapes, many of which are conserved amongst eukaryotes. The morphological dynamics of the lipid bilayer have been shown to play important roles in many cellular processes, be it organelle biogenesis, endocytosis, or vesicular trafficking, and defects have been linked to many diseases. Endoplasmic reticulum (ER) is an organelle with extensive and continuous membrane network. How morphologically different ER domains are formed is not clear. Investigations of ER shaping and remodeling have led to the discovery of two groups of membrane proteins: the reticulons and DP1/Yop1p, proteins that are both necessary and sufficient for the generation of ER tubules; and a class of membrane-bound, dynamin-like GTPases, called atlastins, which appear to have a role in the fusion of ER membranes. Our recent structural and biochemical studies of atlastin provided first insight into the mechanism underlying ER fusion. We aim to use combined approaches to further investigate the mechanism and regulation of the tubular ER network formation. We are also interested in the functional significance of different ER morphologies, and their implication in various human diseases.
Publications
-
Yan L, Sun S, Wang W, Shi J, Hu X, Wang S, Su D, Rao Z, Hu J, Lou Z. Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion. J Cell Biol. 2015 Sep 14;210(6):961-72.