Yan-Qing Ma, PhD

Associate Investigator
Blood Research Institute
BloodCenter of Wisconsin
Assistant Professor
Department of Biochemistry
Medical College of Wisconsin

Education and Training
Doctoral Training
Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Postdoctoral Training
Lerner Research Institute, Cleveland Clinic
Contact Information
Phone: (414) 937-3881
Fax: (414) 937-6284

Thrombosis, Hemostasis and Vascular Biology
Integrins deliver bidirectional signals (inside-out signaling and outside-in signaling) across the plasma membrane to modulate cell adhesion, migration, proliferation, differentiation and apoptosis. The inside-out signaling is a series of molecular events within cells that eventually lead to integrin activation to allow extracelluar ligand binding. For many integrin members, their activation is tightly controlled by integrin cytoplasmic tail-associating proteins. The interactive cooperation between integrin cytoplasmic tails, tail-associating proteins and local membrane phospholipids defines the final integrin activation state.

The current research project in our laboratory is to identify and characterize the key components in the integrin activation machinery, especially, the integrin tail-associating proteins. Our long-term goal is to interpret the detailed molecular mechanisms of integrin activation and further explore their therapeutic value for vascular disease. To realize such a goal, multiple experimental approaches have been employed in our lab, ranging from basic protein analyses, cellular mechanisms, to small animal models.

GrantsScientist Development Grant, American Heart Association, 2010-2013


Basic Science Grant in Breast Cancer, MCW Cancer Center and the Wisconsin Breast Cancer Showhouse, 2013-2014

Zhen Xu, PhD

Research Scientist I

Jiayi Cai
Postdoctoral Fellow

Selected Publications
  • Ma Y.Q. and Geng JG. Heparan sulfate-like proteoglycans mediate adhesion of human malignant melanoma A375 cells to P-selectin under flow. J. Immunol. 165: 558- 565; 2000.
  • Ma Y.Q. and Geng JG. Obligatory requirement of sulfation for P-Selectin binding to human salivary gland carcinoma Acc-M cells and breast carcinoma ZR-75-30 cells. J. Immunol. 168:1690-1696; 2002.
  • Ma Y.Q., Plow EF and Geng JG. P-selectin Binding to P-selectin Glycoprotein Ligand-1 Induces an Intermediate State of αMβ2 Activationand Acts Cooperatively with Extracellular Stimuli to Support Maximal Adhesion of Human Neutrophils. Blood 104: 2549-2556; 2004.
  • Plow EF, Pesho M and Ma Y.Q. “Integrin αIIbβ3”, chapter 8 in: Platelets 2/e, Michelson, 2007.
  • Ma Y.Q., Yang, J., Pesho, M., Vinogradova O., Qin, J. and Plow EF. Regulation of Integrin alphaIIbbeta3 Activation by Distinct Regions of its Cytoplasmic Tails. Biochemistry 45(21):6656-62; 2006.
  • Ma Y.Q., Qin J and Plow EF. Platelet Integrin αIIbβ3: Activation Mechanisms. Journal of Thrombosis and Haemostasis 5: 1345-1352; 2007.
  • Plow EF and Ma Y.Q. Inside-out, outside-in: what’s the difference? Blood 109(8): 3128-29; 2007.
  • Shi X., Ma Y.Q., Tu Y., Chen K., Wu S., Fukuda K., Qin J., Plow EF and Wu C. Mig-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J. Biol. Chem. 282(28):20455-66; 2007.
  • Ma Y.Q., Qin J., Wu C. and Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 181: 439-446; 2008.
  • Goksoy E.*, Ma Y.Q.*, Wang X., Kong X., Perera D., Plow EF and Qin J. (2008) Structural basis for the autoinhibition of talin in regulating integrin activation. Mol Cell. 31(1):124-33; 2008.
  • Malinin NL, Zhang L., Chio J., Ciocea A., Razorenova O, Ma, Y.Q., Podrez EA, Tosi M., Lennon DP, Caplan AI, Shurin SB, Plow EF and Byzova TV. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nature Medicine 15(3):313-8; 2009.
  • Ithychanda SS, Das M., Ma Y.Q., Ding K., Wang X., Gupta S., Wu C., Plow EF and Qin J. Migfilin: a molecular switch in regulation of integrin activation. J. Biol. Chem. 284(7): 4713-4722; 2009.
  • Plow EF, Ma Y.Q., Byzova TV and Jun Q. Platelet Aggregation: A Brief Historical and Molecular Perspective. Journal of Thrombosis and Thrombolysis 26(1):68-70; 2009.
  • Yang J., Ma Y.Q., Rage RC, Misra S., Plow EF and Qin J. Structure of an integrin αIIbβ3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc Natl Acad Sci U S A. 106(42):17729-34; 2009.
  • Bialkowska K., Ma Y.Q., Bledzka K., Sossey-Alaoui, K., Izem L., Zhang X., Malinin N., Qin J., Byzova T and Plow EF. The integrin co-activator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J. Biol. Chem. 285(24):18640-9; 2010.
  • Bledzka K., Bialkowska K., Nie H., Qin J., Byzova T., Wu, C., Plow EF and Ma Y.Q.* Tyrosine phosphorylation of beta3 integrin regulates kindlin-2 binding and integrin activation. J. Biol. Chem. 285(40):30370-4; 2010.
  • Pluskota E., Dowling JJ, Gordon N., Golden J., Szpak D., West ZX., Nestor C., Ma Y.Q., Bialkowska K., Byzova T and Plow EF. The integrin co-activator kindlin-2 plays a critical role in angiogenesis in mice and zebrafish. Blood 117(18):4978-87; 2011.
  • Perera, H.D., Ma, Y.Q., Yang, J., Hirbawi, J. Plow, E.F., and Qin, J. Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. Structure, 19(11):1664-71; 2011.
  • Liu J., Fukuda K., Xu Z., Ma Y.Q., Hirbawi J., Plow EF and Qin J. Structural basis of phosphoinositide binding to Kindlin-2 pleckstrin homology domain in regulating integrin activation. J. Biol. Chem. 286(50):43334-42; 2011.
  • Bledzka K., Liu J., Xu Z., Perera HD., Yadav SP., Bialkowska K., Qin J., Ma Y.Q.* and Plow EF.* Spatial coordination of kindlin-2 with talin head domain in interaction with integrin β cytoplasmic tails. J. Biol. Chem. 287(29):24585-94. 2012.
  • Bledzka K., Pesho M., Ma, Y.Q., and Plow, E.F.  Integrin αIIbβ3, chapter 8 in: Platelets 3/e. Michelson. 2013.
  • Xu, Z., Gao, J., Hong, J., and Ma, Y.Q.  Integrity of Kindlin-2 FERM subdomains is required for supporting integrin activation.  BBRC.  434(2):382-7.  2013.
  • Pluskota E., Ma, Y., Bledzka, K.M., Bialkoska, K., Soloviev, D.A., Szpak, D., Podrez, E.A., Fox, P.L., Hazen, S.L., Dowling, J.J., Ma, Y.Q. and Plow, E.F.  Kindlin-2 regulates hemostasis by controlling endothelial cell surface expression of ADP/AMP catabolic enzymes via a clathrin-dependent mechanism.   Blood 122(14):2491-9. 2013.

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