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Junjie Hu

Professor
Institute of Biophysics
Chinese Academy of Sciences
China

Biography

2000, B.S. Biochemistry, Fudan University, Shanghai, China 2005, Ph.D., Biomedical Science, New York University 2008, Cell Biology, Postdoctoral, Harvard Medical School/HHMI

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

  • 3. Zhang M, Wu F, Shi J, Zhu Y, Zhu Z, Gong Q, Hu J. ROOT HAIR DEFECTIVE3 family of dynamin-like GTPases mediates homotypic endoplasmic reticulum fusion and is essential for Arabidopsis development. Plant Physiol. 2013 Oct;163(2):713-20.

  • 2. Liu TY, Bian X, Romano FB, Shemesh T, Rapoport TA, Hu J. Cis and trans interactions between atlastin molecules during membrane fusion. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):E1851-60.

  • 1. 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.

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