Jun  Qin,  PhD

Jun Qin, PhD

Staff, Professor of Molecular Medicine

The Bonnie and Eunice Collins Endowed Chair for Innovative Diabetes Research

Lerner Research Institute, 9500 Euclid Avenue, Cleveland, Ohio 44195
Location: NB2-88

Phone: (216) 444-5392


Every living cell in our body is composed of hundreds of thousands of proteins. These proteins are highly coordinated in their functions for regulating diverse cellular processes and thus fundamental to our life. The broad theme of our research is to understand the molecular basis of some key protein-protein interactions in transducing cellular information (cell signaling) and their dysfunctions in human diseases such as heart failure, diabetes, and cancer. To this end, we have been focusing on a class of cell surface receptors, integrins, and their associated proteins. Integrins are major components of cell-extracellular matrix (ECM) adhesion, cell morphology, and cell motility. Using structural biology techniques, including NMR spectroscopy and crystallography, we aim to build a three dimensional atomic level landscape of integrin-mediated protein interaction network to gain thorough understanding of integrin signaling. Our work so far has significantly advanced the field by building key parts of this landscape, which provided important mechanistic insight into the mechanisms of integrin signaling. In collaboration with a group of cell biologists and clinical scientists, we also investigate other important cellular signaling pathways and their dysregulations. We have been able to link our recent atomic level findings to the pathogenesis of several human disorders with exciting identification of several potential protein inhibitors for these disorders. Our studies may ultimately help develop better approaches for diagnosing and treating the relevant human diseases.

Vinogradova, O., et al. A structural mechanism of integrin αIIbβ3 ‘inside-out’ activation as regulated by its cytoplasmic face. Cell, 110, 587-597, 2002.

Vaynberg, J. et al. Structure of an ultra weak protein-protein complex and its crucial role in regulation of cell morphology and motility. Molecular Cell, 17:513-523,2005.

Goksoy, E., et al. Structural basis for the autoinhibition of talin in regulating integrin activation. Molecular Cell,31:124-133, 2008. 

Fukuda, K. et al. The pseudo active site of ILK is essential for its binding to a-parvin and localization to focal adhesions. Molecular Cell, 36:819-830, 2009.

Yang, J., et al. Structure of an integrin αIIbβ3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc. Natl. Acad. Sci. 106:17729-34, 2009.

Song X., et al. A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion. Cell Research 22:1533-45, 2012.

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