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


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.

Selective Publications:

  1. Vinogradova, O., Velyvis, A., Velyviene, A., Hu, B., Haas, T., Plow, E.F., and Qin, J. A structural mechanism of integrin aIIbb3 ‘inside-out’ activation as regulated by its cytoplasmic face. Cell, 110, 587-597, 2002.
  2. Velyvis A, Vaynberg, J., Yang, Y., Vinogradova O, Zhang, Y., Wu, C., Qin J. Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling Nature Struct. Biol., 10, 558-564, 2003.
  3. Vaynberg, J., Fukuda, T., Chen, K., Vinogradova, O., Velyvis, A., Tu, Y., Ng, L., Wu, C. and Qin, J. Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility. Molecular Cell, 17:513-523, 2005.
  4. Goksoy, E., Ma, Y.Q., Kong, X., Perera, D., Plow, E.F., and Qin, J. Structural basis for the autoinhibition of talin in regulating integrin activation. Molecular Cell, 31:124-33, 2008.
  5. Fukuda, K., Gupta, S., Chen, K., Wu, C., and Qin, J. 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.
  6. Yang, J., Zhu, L., Zhang, H., Hirbawi, J., Fukuda, K., Dwivedi, P., Liu, J., Byzova, T.V., Plow, E.F., Wu, J., and Qin, J. Conformational activation of talin by RIAM triggers integrin-mediated cell adhesion, Nature Communications, 5:5880, 2014.
  7. Liu, J., Das, M., Yang, J., Ithychanda, S.S., Yakubenko, V.P., Plow, E.F., and Qin, J. Structural mechanism of integrin inactivation by filamin. Nature Struct Mol Biol, 22:383-389, 2015.
  8. Zhu, L., Yang, J., Bromberger, T., Holly, A., Lu, F., Liu, H., Sun, K., Klapproth, S., Hirbawi, J., Byzova, T.V., Plow, E.F., Moser, M., and Qin, J. Structure of Rap1b bound to talin reveals a new pathway for triggering integrin activation. Nature Communications, 8:1744, 2017.
  9. Vaynberg, J., Fukuda, K., Lu, F., Bialkowska, K., Chen, Y., Plow, E.F., and Qin, J. Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion. Nature Communications, 9:4465, 2018.
  10. Lu, F., Zhu, L., Bromberger, T., Yang, J., Yang, Q., Liu, J., Plow, E.F., Moser, M., and Qin, J. Mechanism of integrin activation by talin and its cooperation with kindlin. Nature Communications, 13(1):2362, 2022.

See the complete publication list: