Dr. Jin's interest is in the role of the NMDA receptor in synaptic plasticity and memory formation, and in brain injury and disease.
Dr. Jin received his Ph.D. from Columbia University, for his work on the structure and function of glutamate receptors.
Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.
Gu S, Rumpel S, Zhou J, Strotmeier J, Bigalke H, Perry K, Shoemaker CB, Rummel A, Jin R
Science. 2012 Feb 24;335(6071):977-81
Structural basis of agrin-LRP4-MuSK signaling.
Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, Figueiredo D, Perry K, Mei L, Jin R
Genes Dev. 2012 Feb 1;26(3):247-58
Crystal structure of the glutamate receptor GluA1 N-terminal domain.
Yao G, Zong Y, Gu S, Zhou J, Xu H, Mathews II, Jin R
Biochem J. 2011 Sep 1;438(2):255-63
The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites.
Strotmeier J, Gu S, Jutzi S, Mahrhold S, Zhou J, Pich A, Eichner T, Bigalke H, Rummel A, Jin R, Binz T
Mol Microbiol. 2011 Jul;81(1):143-56
Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner.
Strotmeier J, Lee K, Völker AK, Mahrhold S, Zong Y, Zeiser J, Zhou J, Pich A, Bigalke H, Binz T, Rummel A, Jin R
Biochem J. 2010 Oct 15;431(2):207-16
The N-terminal domain of GluR6-subtype glutamate receptor ion channels.
Kumar J, Schuck P, Jin R, Mayer ML
Nat Struct Mol Biol. 2009 Jun;16(6):631-8
Crystal structure and association behaviour of the GluR2 amino-terminal domain.
Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, Zhou J, Jin Y, Gouaux E
EMBO J. 2009 Jun 17;28(12):1812-23
Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity.
Jin R, Sikorra S, Stegmann CM, Pich A, Binz T, Brunger AT
Biochemistry. 2007 Sep 18;46(37):10685-93
Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity.
Jin R, Rummel A, Binz T, Brunger AT
Nature. 2006 Dec 21;444(7122):1092-5
Mechanism of positive allosteric modulators acting on AMPA receptors.
Jin R, Clark S, Weeks AM, Dudman JT, Gouaux E, Partin KM
J Neurosci. 2005 Sep 28;25(39):9027-36
Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase.
Jin R, Junutula JR, Matern HT, Ervin KE, Scheller RH, Brunger AT
EMBO J. 2005 Jun 15;24(12):2064-74
Structural basis for partial agonist action at ionotropic glutamate receptors.
Jin R, Banke TG, Mayer ML, Traynelis SF, Gouaux E
Nat Neurosci. 2003 Aug;6(8):803-10
View All Publications
Amino Acid Metabolism is Altered in Adolescents with Nonalcoholic Fatty Liver Disease-An Untargeted, High Resolution Metabolomics Study.
Jin R, Banton S, Tran VT, Konomi JV, Li S, Jones DP, Vos MB
J Pediatr. 2016 Feb 5;
Prostaglandins E2 signal mediated by receptor subtype EP2 promotes IgE production in vivo and contributes to asthma development.
Gao Y, Zhao C, Wang W, Jin R, Li Q, Ge Q, Guan Y, Zhang Y
Sci Rep. 2016;6:20505
Rongsheng Jin's Research Focus
Alzheimer's Disease, Amyotrophic Lateral Sclerosis (Lou Gehrig's Disease)
The brain is a massive network of electrically active cells (neurons) that communicate with each other by synaptic transmission at specialized intercellular junctions called synapses. Ionotropic glutamate receptors (iGluRs) are the major mediators of excitatory synaptic transmission in the central nervous system (CNS). The N-methyl-D-aspartate subtype of glutamate receptor (NMDAR) has attracted particular interest because of its unique role in synaptic plasticity, memory formation and disease. Excessive activation of NMDARs has been associated with neuronal cell injury and death in hypoxic-ischemic brain injury, trauma and epilepsy, and several degenerative neurological disorders such as Huntington’s disease, amyotrophic lateral sclerosis, HIV dementia, Alzheimer’s disease and Parkinson’s disease. Dr. Jin’s research focuses on elucidating the molecular basis underlying NMDAR regulation and functional plasticity using a combination of biochemical, biophysical, and electrophysiological approaches. These studies will facilitate the design and improvement of therapeutic agents for the treatment of psychological and neurological disorders. A second area of research concerns the structure and function of botulinum neurotoxins (BoNTs), which are among the most poisonous substances known to man. BoNTs therefore represent a major bioterrorist threat. Paradoxically, BoNT-containing medicines and cosmetics, such as Botox® and Dysport®, have been used with great success in clinic. Both the toxic and therapeutic functions of BoNTs indeed rely on a common mechanism to enter neurons, cleave proteins that mediate exocytosis of key neurotransmitters, and subsequently paralyze the affected muscles. The Jin laboratory is attempting to understand the molecular mechanisms underlying the BoNT-host interplay during the course of intoxication. Specifically, Dr. Jin and his colleagues are interested in two major questions: (1) How does BoNT survive the harsh environment (low pH, protease-rich) of the gastrointestinal tract and penetrate gut epithelial cells to reach the general circulation? (2) How does BoNT recognize and invade nerve cells at neuromuscular junctions? A better understanding of these fundamental questions will guide the development of effective anti-BoNT strategies, will help improve clinical efficacy of BoNT-containing drugs, and will suggest novel applications for BoNT.
About Rongsheng Jin
Rongsheng Jin earned his Ph.D. in the group of Dr. Eric Gouaux at Columbia University, for his work on the structure and function of glutamate receptors. He conducted his postdoctoral research in the laboratory of Dr. Axel Brunger at Stanford University, where he focused on the structural studies of the Sec6/8 complex (exocyst) and botulinum neurotoxins (BoNTs). He joined the faculty of Sanford-Burnham Medical Research Institute as an adjunct assistant professor in January 2007, and later assistant professor in September 2007. Dr. Jin is the recipient of the Alfred P. Sloan Research Fellowship and the HFSP (Human Frontier Science Program) Young Investigator research grant.