Abstract

There are currently three studies within this project: 1) Transient kinetics of the sodium pump: Investigations into the cause of the biphasic characteristics of catalytic site phosphorylation and dephosphorylation, in collaborations with Froehlich, Fendler and Taniguchi. 2) Regulatory modifications of the sodium pump: Current studies are directed toward testing the hypothesis that the great sensitivity of P-type cation pumps to certain solvents is an """"""""osmotic stress"""""""" effect on the accessibility of water to certain sites in these pump molecules. 3) Regulatory modifications of calmodulin-dependent kinase II: Studies of the functional consequences of the autophosphorylation states of calmodulin-dependent kinase II, in collaboration with A. Dosemeci.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Intramural Research (Z01)
Project #
1Z01NS000813-35
Application #
2579498
Study Section
Special Emphasis Panel (LNC)
Project Start
Project End
Budget Start
Budget End
Support Year
35
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
National Institute of Neurological Disorders and Stroke
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

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