Abstract

This project is comprised of research into the structure and functioning of ion transport systems. There are currently three active subprojects: 1) Transient kinetics: A collaborative study with Froehlich and Fendler on the source of the transmembrane current that is generated by phosphorylation of the sodium pump has been completed. Collaboration with Froehlich on the source of the biphasic characteristics of phosphorylation and dephosphorylation is continuing. 2) Investigation of posttranslational modifications of the sodium pump. This project involves characterization of identified fragments of the sodium pump catalytic subunit by mass spectrometry. 3) Studies of the effects of kinase and phosphatase inhibitors and activators on sodium pump activity. These are studies carried out on preparations that will be correlated with the work in subproject #2.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Intramural Research (Z01)
Project #
1Z01NS000813-32
Application #
3782278
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
32
Fiscal Year
1993
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