金香淑博士
- 基本信息
- 教育经历
- 工作经历
- 研究概述
- 发表文章
金香淑 博士
北京生命科学研究所研究员
Xiangshu Jin, Ph.D. Former Assistant Investigator, NIBS, Beijing，China
Phone：86-10-80726688
Fax： 86-10-80726689
E-mail：jinxiangshu@nibs.ac.cn
教育经历
Education
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2002年 |
美国密歇根州立大学化学博士 |
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Ph. D., Chemistry, Michigan State University, East Lansing, MI, USA |
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1995年 |
北京大学化学学士 |
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B.S., Chemistry, Peking University, Beijing, China |
工作经历
Professional Experience
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2012- |
北京生命科学研究所研究员 |
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Assistant Investigator, National Institute of Biological Sciences, Beijing, China |
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2007-2012年 |
美国霍华德休斯医学研究所/哥伦比亚大学生物化学与分子生物物理系副研究员 |
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Research Specialist, Howard Hughes Medical Institute; Adjunct Associate Research Scientist, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA |
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2006-2007年 |
美国哥伦比亚大学生物化学与分子生物物理系副研究员 |
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Associate Research Scientist, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA |
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2003-2006年 |
美国哈佛大学分子与细胞生物学系博士后 |
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Postdoctoral Research Fellow, Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, USA |
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2003年 |
美国密歇根州立大学生物化学与分子生物学系博士后 |
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Postdoctoral Research Scientist, Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA |
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1995-1998年 |
北京大学考古文博学院助教 |
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Assistant, Conservation Laboratory, School of Archaeology and Museology, Peking University, Beijing, China |
研究概述
Research Description
我们实验室的研究兴趣在于生物模式形成(biological pattern formation)所必需的细胞间通讯的分子机制。在具有特定功能的各种生物模式的形成过程中，细胞表面受体与相邻细胞表达的配体分子特异性地相互作用。表面受体将这些细胞外的分子信号跨膜转导至细胞内，从而启动细胞内信号转导的级联反应，以达到相邻细胞之间功能上的相互协调。我们综合运用结构生物学、生物物理、生物化学、细胞生物学、计算生物学等多种手段，在原子和分子水平上探索有关受体与配体之间特异性相互作用的机理，并延伸到细胞乃至系统水平上研究和阐明各种生物模式的形成机制。实验室目前的研究主要集中在平面细胞极性(planar cell polarity)建立的分子机制，我们将着力研究CELSR亚家族的粘附G蛋白偶联受体及其相关粘附受体所介导的细胞间相互作用的分子机制、受体的激活机制、以及下游分子信号通路。
Our laboratory is interested in understanding the molecular “languages” of cell-cell communication that coordinates biological pattern formation. Formation of multicellular patterns associated with specific biological functions entails intricate communication networks whereby cells talk to each other through specific interactions between surface receptors and ligands presented from neighboring cells. These extracellular molecular cues are then transduced into appropriate intracellular responses, which allow a group of cells to coordinate their activities and collectively form elaborate multicellular patterns. We use a multidisciplinary approach combining structural biology, biophysics, biochemistry, cell biology, and computational biology to study the mechanisms of biological pattern formation at the atomic, molecular, cellular, and systems levels.
Our current efforts are focused on understanding the molecular interactions that underlie the establishment of planar polarity, a form of multicellular organization that coordinates polarization of cells within a tissue plane and iscritical for diverse developmental processes. To this end, we take a multipronged approach to study the extracellular interactions mediated by the CELSR family adhesion GPCRs and related adhesion receptors, the activation mechanisms of these receptors, and their downstream signaling pathways.
发表文章
Publications
Peer-reviewed research articles:
1. Cao Y*, Pan Y*, Huang H*, Jin X, Levin EJ, Kloss B, Zhou M (2013) Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature 496, 317-322.(*equal contribution)
2. Harrison OJ, Vendome J, Brasch J, Jin X, Hong S, Katsamba PS, Ahlsen G, Troyanovsky RB, Troyanovsky SM, Honig B, Shapiro L (2012) Nectin ectodomain structures reveal a canonical adhesive interface. Nature Structural and Molecular Biology 906-915.
3. Glaaser IW, Osteen JD, Puckerin A, Sampson KJ, Jin X, Kass RS (2012)Perturbation of sodium channel structure by an inherited long QT Syndrome mutation. Nature Communications 3, 706.
4. Jin X*, Walker MA*, Felsovalyi K*, Vendome J*, Bahna F, Mannepalli S, Cosmanescu F, Ahlsen G, Honig B, Shaprio L (2012) Crystal structures ofDrosophila N-cadherin ectodomain regions reveal a widely used class of Ca2+-free interdomain linkers. Proc. Natl. Acad. Sci. U.S.A. 109, E127-134. (*equal contribution)
5. Vendome J*, Posy S*, Jin X, Bahna F, Ahlsen G, Shapiro L, Honig B (2011)Molecular design principles underlying β-strand swapping in the adhesive dimerization of cadherins. Nature Structural and Molecular Biology 18, 693-700. (*equal contribution)
6. Cao Y, Jin X*, Levin EJ*, Huang H*, Zong Y*, Quick M, Weng J, Pan Y, Love J, Punta M, Rost B, Hendrickson WA, Javitch JA, Zhou M (2011) Crystal structure of a phosphorylation-coupled saccharide transporter. Nature 473, 50-54.(*equal contribution)
7. Cao Y*, Jin X*, Huang H*, Derebe MG, Levin EJ, Kabaleeswaran V, Pan Y, Punta M, Love J, Weng J, Quick M, Ye S, Kloss B, Bruni R, Martinez-Hackert E, Hendrickson WA, Rost B, Javitch JA, Rajashankar KR, Jiang Y, Zhou M (2011) Crystal structure of a potassium ion transporter TrkH. Nature 471, 336-340. (*equal contribution)
8. Harrison OJ*, Jin X*, Hong S, Bahna F, Ahlsen G, Brasch J, Wu Y, Vendome J, Felsovalyi K, Hampton CM, Troyanovsky RB, Ben-Shaul A, Frank J, Troyanovsky SM, Shapiro L, Honig B (2011) The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure 19, 244-256. (*equal contribution)
9. Wu Y, Jin X, Harrison O, Shapiro L, Honig BH, Ben-Shaul A. (2010) Cooperativity between trans and cis interactions in cadherin-mediated junction formation. Proc. Natl. Acad. Sci. U.S.A. 107, 17592-17597.
10.Koehnke J*, Katsamba PS*, Ahlsen G, Bahna F, Vendome J, Honig B, Shapiro L,Jin X* (2010) Splice form dependence of beta-neurexin/neuroligin binding interactions. Neuron 67, 61-74. (*equal contribution)
11.Harrison OJ, Bahna F, Katsamba PS, Jin X, Brasch J, Vendome J, Ahlsen G, Carroll KJ, Price SR, Honig B, Shapiro L (2010) Two-step adhesive binding by classical cadherins. Nature Structural and Molecular Biology 17, 348-357.
12.Ciatto C, Bahna F, Zampieri N, VanSteenhouse HC, Katsamba PS, Ahlsen G, Harrison OJ, Brasch J, Jin X, Posy S, Vendome J, Ranscht B, Jessell TM, Honig B, Shapiro L (2010) T-cadherin structures reveal a novel adhesive binding mechanism. Nature Structural and Molecular Biology 17, 339-347.
13.Koehnke J, Jin X, Trbovic N, Katsamba PS, Brasch J, Ahlsen G, Scheiffele P, Honig B, Palmer AG 3rd, Shapiro L (2008) Crystal structures of β-neurexin 1 and β-neurexin 2 ectodomains and dynamics of splice insertion sequence 4.Structure 16, 410-421.
14.Koehnke J*, Jin X*, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L(2008) Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. Proc. Natl. Acad. Sci. U.S.A. 105, 1873-1878. (*equal contribution)
15.Jin X, Townley R, Shapiro L (2007) Structural insight into AMPK regulation: ADP comes into play. Structure 15, 1285-1295.
16.Lishko PV*, Procko E*, Jin X*, Phelps CB, Gaudet R (2007) The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54, 905-918. (*equal contribution)
17.Jin X, Touhey J, Gaudet R (2006) Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 281, 25006-25010.
18.Bejar CM, Jin X, Ballicora MA, Preiss J (2006) Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases. J. Biol. Chem.281, 40473-40484.
19.Jin X, Ballicora MA, Preiss J, Geiger JH (2005) Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO J. 24, 694-704.
20.Jin X, Foley KM, Geiger JH (2004) The structure of the
21.Jin X, Geiger JH (2003) Structures of NAD+-and NADH-bound 1-L-myo-inositol 1-phosphate synthase. Acta. Crystallogr. Sect. D: Biol. Crystallogr.59, 1154-1164.
Invited reviews and book chapters:
1. Rohs R*, Jin X*, West SM, Joshi R, Honig B, Mann RS (2010) Origins of specificity in protein-DNA recognition. Annu. Rev. Biochem. 79, 233-269. (*co-first authors)
2. Geiger JH, Jin X (2006) The structure and mechanism of myo-inositol-1-phosphate synthase. Subcell. Biochem. 39, 157-180.
