The principal goal of this project is to elucidate function of the sodium pump, in particular we are interested in the transient kinetics of the sodium pump. A collaboration with J. Froehlich of NIA is directed at determining the extent to which oligomeric interactions of the sodium pump contribute to the efficiency of cation transport. We have obtained evidence, by a variety of techniques, that """"""""out-of-phase"""""""" interactions of two or more alpha subunits occur in the native state of this and other P-type cation pumps.

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Intramural Research (Z01)
Project #
1Z01NS000813-39
Application #
6432872
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
39
Fiscal Year
2000
Total Cost
Indirect Cost
City
State
Country
United States
Zip Code
Rudrabhatla, Parvathi; Zheng, Ya-Li; Amin, Niranjana D et al. (2008) Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein. J Biol Chem 283:26737-47
Amin, Niranjana D; Zheng, Ya-Li; Kesavapany, Sashi et al. (2008) Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis. J Neurosci 28:3631-43
Kesavapany, Sashi; Patel, Vyomesh; Zheng, Ya-Li et al. (2007) Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons. Mol Biol Cell 18:3645-55
Mahaney, James E; Albers, R Wayne; Waggoner, Jason R et al. (2005) Intermolecular conformational coupling and free energy exchange enhance the catalytic efficiency of cardiac muscle SERCA2a following the relief of phospholamban inhibition. Biochemistry 44:7713-24
Mahaney, James E; Albers, R Wayne; Kutchai, Howard et al. (2003) Phospholamban inhibits Ca2+ pump oligomerization and intersubunit free energy exchange leading to activation of cardiac muscle SERCA2a. Ann N Y Acad Sci 986:338-40
Amin, Niranjana D; Albers, Wayne; Pant, Harish C (2002) Cyclin-dependent kinase 5 (cdk5) activation requires interaction with three domains of p35. J Neurosci Res 67:354-62
Zheng, Ya-Li; Li, Bing-Sheng; Amin, Niranjana D et al. (2002) A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells. Eur J Biochem 269:4427-34