and Training Goals I am interested in the dynamic binding interactions between membrane proteins. How do they interact, and how tightly and rapidly do they bind and unbind? How do these interactions affect protein function? I propose to develop new techniques to answer these questions, including a new way to measure binding/unbinding rates, and a new research tool called a """"""""biomimetic endoplasmic reticulum."""""""" Development of these new technologies will require an intensive period of training in biomedical engineering and kinetics. This additional training will greatly enhance my professional preparation for a career as an independent research scientist. Relevance to Public Health The goals of this research project are important, both in terms of the model proteins studied directly, and in terms of the proposed technical advancement of the study of membrane proteins generally. Disorders of the SERCA pump and its regulation by phospholamban have been correlated to disease, including heart failure. By understanding how these proteins work we might develop drugs or other clinical therapies to intervene in the disease process. Furthermore, the technical developments I propose are likely to be generally applicable to the study of many other clinically important membrane proteins.

National Institute of Health (NIH)
National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Research Scientist Development Award - Research & Training (K01)
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Study Section
Special Emphasis Panel (ZEB1-OSR-A (O1))
Program Officer
Erim, Zeynep
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Loyola University Chicago
Schools of Medicine
United States
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Pallikkuth, Sandeep; Blackwell, Daniel J; Hu, Zhihong et al. (2013) Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase. Biophys J 105:1812-21
Xu, Li; Pallikkuth, Sandeep; Hou, Zhanjia et al. (2011) Dysferlin forms a dimer mediated by the C2 domains and the transmembrane domain in vitro and in living cells. PLoS One 6:e27884
Ha, Kim N; Masterson, Larry R; Hou, Zhanjia et al. (2011) Lethal Arg9Cys phospholamban mutation hinders Ca2+-ATPase regulation and phosphorylation by protein kinase A. Proc Natl Acad Sci U S A 108:2735-40
Song, Qiujing; Pallikkuth, Sandeep; Bossuyt, Julie et al. (2011) Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase. J Biol Chem 286:9120-6
Bidwell, Philip; Blackwell, Daniel J; Hou, Zhanjia et al. (2011) Phospholamban binds with differential affinity to calcium pump conformers. J Biol Chem 286:35044-50
Hou, Zhanjia; Robia, Seth L (2010) Relative affinity of calcium pump isoforms for phospholamban quantified by fluorescence resonance energy transfer. J Mol Biol 402:210-6
Koshman, Yevgeniya E; Kim, Taehoon; Chu, Miensheng et al. (2010) FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 30:2226-33
Zhao, Wen; Waggoner, Jason R; Zhang, Zhi-Guo et al. (2009) The anti-apoptotic protein HAX-1 is a regulator of cardiac function. Proc Natl Acad Sci U S A 106:20776-81
Bossuyt, Julie; Despa, Sanda; Han, Fei et al. (2009) Isoform specificity of the Na/K-ATPase association and regulation by phospholemman. J Biol Chem 284:26749-57
Hou, Zhanjia; Kelly, Eileen M; Robia, Seth L (2008) Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex. J Biol Chem 283:28996-9003

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