Qian Yin

My lab is interested in how individual proteins, or protein assemblies, mediate biological processes in the linked areas of membrane trafficking, innate immunity, and host-pathogen interactions. Longer-term perspectives extend to the interplay between inflammation, infection, autophagy, and cytoskeleton rearrangement. We study the mechanisms of pathogen-associated molecular patterns (PAMPs) recognition, viral restriction, evasion or suppression of host immunity and their intricate network using a combination of biochemical, structural (including X-ray crystallography and cryo-EM), cellular and pharmacological approaches. Mechanistic and structural studies of IFN-inducible GTPases GTPases have been meticulously documented for their roles to regulate multiple cellular processes spanning from cell mobility, membrane fusion and fission, to cytokinesis and vesicle transport. IFN-inducible GTPases, consisting of more than forty members in human and mice, are conserved from vertebrates to human. They are among the most highly expressed ISGs, sometimes accounting for twenty percent of all proteins induced by IFN-γ. Yet the functions of IFN-inducible GTPases remain largely unknown. IFN-inducible GTPases can be classified into three major subfamilies: guanylate-binding proteins (GBPs), immunity-related GTPases (IRGs), and myxovirus resistance (Mx) proteins. IRGs can be further divided into GKS and GMS IRGs based on sequence features. They are all part of cell-autonomous resistance against microbial infections by patrolling the intracellular space, targeting pathogen-containing vacuoles (PVs) and viruses, promoting inflammasome formation, and coordinating assembly of oxidative and autophagic complexes for wide-spectrum pathogens elimination. I propose to study the working mechanisms and structure-function relationships of GBPs and IRGs. 1. Elucidating GBP self-organization by biochemical, structural and microscopic methods 2. Understanding the specificity of GBPs and IRGs towards foreign entities 3. Revealing the pathogen counterattack strategies Highly motivated individuals are welcome to contact Dr. Yin for positions at all levels: undergraduate student researchers, graduate students, postdoctoral fellows, and technicians.

Wang B, Yang R, Wan C, Tian Y, Wu J, Adewole TS, Roy S, Li S, Shen J*, and Yin Q*. Structural basis of pseudoGTPase-mediated protein-protein interaction. Structure. 2025; [DOI] Online ahead of print Roy S, Wang B, Roy K, Tian Y, Bhattacharya M, Williams S, and Yin Q. Crystal structures reveal nucleotide-induced conformational changes in G motifs and distal regions in human guanylate-binding protein 2. Commun Biol. 2025; 8(1):282 [Commun Biol] [PMC11846989] Wan C, Puscher H, Ouyang Y, Wu J, Tian Y, Li S, Yin Q*, and Shen J*. An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex. Proc Natl Acad Sci USA. 2024; 121(34):e2409341121 [PNAS] [PMC11348294] Bhattacharya M, Bhowmik D, Tian Y, He H, Zhu F, and Yin Q. The Dengue virus protease NS2B3 cleaves cyclic GM