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Scientist Emeritus

Harish C. Pant, Ph.D.

Neuronal Cytoskeletal Protein Regulation Section

Laboratory of Neurochemistry, NINDS
Building 49 Room 2A35
49 Convent Drive MSC 4479
Bethesda MD 20892-4479
Office: (301) 402-2124
Lab: (301) 402-2124
Fax: (301) 496-1339

Dr. Pant received his M.A. and Ph.D. degrees in Physics from Agra University, Agra, India. His postdoctoral studies were conducted on the mechanisms of electron and ion transport in model membrane systems at the Department of Biophysics at Michigan State University. He joined the Laboratory of Neurobiology in the NIMH as a senior staff fellow in 1974 with Dr. Ichiji Tasaki where he studied the function of the axonal cytoskeleton in the squid giant axon. In 1979 he moved to the NIAAA extending his studies on the neuronal cytoskeleton and the effects of alcohol on its regulation. Dr. Pant moved to the NINDS in 1987 and retired in 2019 as Chief of the Neuronal Cytoskeletal Protein Regulation Section and was appointed a Scientist Emeritus. His research focused on studying the mechanisms of topographic regulation of neuronal cytoskeleton proteins by post-translational modification, including the role of kinase cascades in normal brain and during neurodegeneration.

The major focus of his research has been to study the mechanisms of topographic regulation of neuronal cytoskeletal proteins regulation by phosphorylation and neurodegeneration. In a normal physiological state, cytoskeletal proteins are phosphorylated extensively in the axonal compartment of a mature neuron. Although all the substrates, kinases, phosphatases and their regulators are synthesized in neuronal cell bodies, little or no cytoskeletal protein phosphorylation has been detected in the cell body compartment. Under a variety of neuropathological conditions, however, such as ALS, Alzheimers Disease, or Picks disease, hyperphosphorylation of these molecules has been found in abnormal aggregates within cell bodies, usually correlated with massive neuronal cell death. The mechanisms underlying these profound compartmental shifts in neuronal phosphorylation are not well understood. The normal physiological processes within neurons are controlled by signal transduction mechanisms that regulate the balance between protein kinase and protein phosphatase activities. With his lab, he has shown that the most abundant and extensively phosphorylated motifs in the c-terminal domains (lys-ser-pro-, or KSP) are primarily phosphorylated by proline directed kinases, cdk5 and MAP kinases. Moreover, they have demonstrated that this phosphorylation is due to activation of the signal transduction cascade. In more recent years, the lab focused on the other part of this regulation, the protein phosphatases. The other project is to study the expression, regulation and role of neuronal Cdk5 in nerve cell function.Cdk5 is a unique multifunctional kinase. Unlike other cyclin-dependent kinases, it is expressed predominantly in post-mitotic neurons, its activity modulated by association with nervous system-specific propeins. Since its identification and characterization in the laboratory, they have been intensively studying its mechanisms of regulation and its role in nerve cell function.

Staff Image
  • Niranjana Amin, Ph.D.

    (301) 496-1673

  • Phil Grant, Ph.D.

  • Bing Li, Ph.D.

    (301) 435-9252

  • Yali Zheng, Ph.D.
    Research Fellow
    (301) 435-9252

  • 1) Amin ND, Zheng YL, Kesavapany S, Kanungo J, Guszczynski T, Sihag RK, Rudrabhatla P, Albers W, Grant P, Pant HC. (2008)
  • Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis.
  • J Neurosci., 28(14), 3631-43
  • 2) Pareek TK, Keller J, Kesavapany S, Agarwal N, Kuner R, Pant HC, Iadarola MJ, Brady RO, Kulkarni AB. (2007)
  • Cyclin-dependent kinase 5 modulates nociceptive signaling through direct phosphorylation of transient receptor potential vanilloid 1.
  • Proc Natl Acad Sci U S A, 104(2), 660-5
  • 3) Kino T, Ichijo T, Amin ND, Kesavapany S, Wang Y, Kim N, Rao S, Player A, Zheng YL, Garabedian MJ, Kawasaki E, Pant HC, Chrousos (2007)
  • Cyclin-dependent kinase 5 differentially regulates the transcriptional activity of the glucocorticoid receptor through phosphorylation: clinical implications for the nervous system response to glucocorticoids and stress.
  • Mol Endocrinol., 21(7), 1552-68
  • 4) Kesavapany S, Patel V, Zheng YL, Pareek TK, Bjelogrlic M, Albers W, Amin N, Jaffe H, Gutkind JS, Strong MJ, Grant P, Pant HC. (2007)
  • Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons.
  • Mol Biol Cell, 18(9), 3645-55
  • 5) Kanungo J, Li BS, Goswami M, Zheng YL, Ramchandran R, Pant HC. (2007)
  • Cloning and characterization of zebrafish (Danio rerio) cyclin-dependent kinase 5.
  • Neurosci Lett., 412(3), 233-8
  • 6) Zheng YL, Li BS, Kanungo J, Kesavapany S, Amin N, Grant P, Pant HC. (2007)
  • Cdk5 Modulation of mitogen-activated protein kinase signaling regulates neuronal survival.
  • Mol Biol Cell., 18(2), 404-13
  • 7) Kesavapany S, Pareek TK, Zheng YL, Amin N, Gutkind JS, Ma W, Kulkarni AB, Grant P, Pant HC. (2007)
  • Neuronal nuclear organization is controlled by cyclin-dependent kinase 5 phosphorylation of Ras Guanine nucleotide releasing factor-1.
  • Neurosignals, 15(4), 157-73
  • 8) Sihag RK, Inagaki M, Yamaguchi T, Shea TB, Pant HC. (2007)
  • Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments.
  • Exp Cell Res., 313(10), 2098-109
  • 9) Kesavapany S, Zheng YL, Amin N, Pant HC. (2007)
  • Peptides derived from Cdk5 activator p35, specifically inhibit deregulated activity of Cdk5.
  • Biotechnol J., 2(8), 978-87
  • 10) Kanungo J, Li BS, Zheng Y, Pant HC. (2006)
  • Cyclin-dependent kinase 5 influences Rohon-Beard neuron survival in zebrafish.
  • J Neurochem., 99(1), 251-9
  • 11) Zheng YL, Kesavapany S, Gravell M, Hamilton RS, Schubert M, Amin N, Albers A, Grant P and Pant HC. (2005)
  • A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons.
  • The EMBO J., 24(1), 209-220
  • 12) Sharma, P., Veeranna, Sharma, M., Amin, N.D., Sihaf, R.K., Grant, P., Ahn, N., Kulkarni, A.B.and pant, H.C. (2002)
  • Phosphorylation of MEK1 by cdk5/p35 down regulates the MAP kinase pathway
  • J. Biol. Chem.
  • 13) Li, B.S.,Wu, Ma, Zhang, Lei, Stenger David A. and Pant, H. C. (2001)
  • Activation of phosphatidylinositol 3-kinase (PI-3K) and extracellular regulated kinases (Erk1/2) is involved in muscarinic receptor-mediated DNA synthesis in progenitor cells.
  • J. Neuroscience, 21, 1569-1579
  • 14) Li B-S, Ma W, Zhang L, Barker JL, Stenger DA, Pant HC (2001)
  • Activation of phosphatidylinositol-3 kinase (P1-3K) and extracellular regulated kinases (Erk 1/2) is involved in muscrinic receptor-mediated DNA synthesis in neural progenitor cells
  • J. Neurosci, 21, 1569-1579
  • 15) Li, B.S., Zhang, L., GU, J., Amin, N.D and Pant, H.C. (2000)
  • Integrin a1b1-mediated activation of cyclin-dependent kinase5 (cd (cdk5 activation of cyclin-dependent kinase 5 activity is involved in neurite out growth and human neurofilament protein H lys-ser-pro tail domain phosphorylation
  • J. Neuroscience, 20, 6055-6062
  • 16) Ma W, Maric D, Li BS, Hu Q, Andreadis JD, Grant GM, Liu QY, Shaffer KM, Chang YH, Zhang L, Pancrazio JJ, Pant HC, Stenger DA, Barker JL (2000)
  • Acetylcholine stimulates cortical precursor cell proliferation in vitro via muscarinic receptor activation and MAP kinase phosphorylation
  • Eur J Neurosci , 12, 1-1240
  • 17) Sharma, P., Steinbach, P.J., Sharma, M., Amin, N.D., Barchi, J.J.and Pant, H.C. (1999)
  • Identification of substrate binding site of cyclin dependent kinase-5
  • J. Biol.Chem., 274, 9600-9606
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