Sankar Ghosh

Not to be confused with Shankar Ghosh.
Sankar Ghosh
Born Calcutta, India
Nationality Indian American
Alma mater Calcutta University
Yeshiva University
Occupation Chair department of microbiology, Columbia University Medical Center (2008–)
Known for Work on transcription factor NF-κB

Sankar Ghosh is an Indian immunologist and microbiologist, who is the chair of the Department of Microbiology & Immunology at Columbia University Medical Center.[1] Previously he has remained a Professor of Immunobiology, Molecular biophysics and Biochemistry, and Molecular, Cellular & Developmental biology, and researcher working at Yale University for 17 years.

Sankar Ghosh's particular area of research is focused on the activation of cellular responses via the inducible transcription factor, NF-κB.


Education

Sankar Ghosh was born and brought up in Calcutta, now Kolkata, from where he did his BSc, MSc, Calcutta University, India, 1981; M.S. Albert Einstein College of Medicine, New York (Yeshiva University), 1984; He received his PhD, from Albert Einstein College of Medicine, New York, in 1988, and thereafter he did his postdoctoral work at the Whitehead Institute, Cambridge, Massachusetts (MIT), under the supervision of Nobel laureate David Baltimore (1989–1991).[2]

Career

A Fellow of Irvington Institute for Medical Research; he joined Yale University faculty, in 1991, and worked there for the next 17-year as Professor of Immunobiology; Molecular, Cellular, and Developmental Biology; and Molecular Biophysics and Biochemistry at Yale University School of Medicine, till he moved to Columbia University in 2008, where he became Chair Department of Microbiology at Columbia University Medical Center.[3]

In 2002, he was named a Howard Hughes Medical Investigator by Howard Hughes Medical Institute.[2] He was also awarded the Ranbaxy Science Foundation's Annual Research Awards for the year 2005, the foundation is a non-profit organisation set-up by Ranbaxy Laboratories Limited (RLL).,[4] then in 2007 he was named as a Fellow of the AAAS, by the American Association for the Advancement of Science (AAAS), for "distinguished contributions to the field of immunology, particularly for studies of the NF-êB signaling pathway." .[5]

Dr. Ghosh has served in an advisory capacity for several organisations, including the Board of Scientific Counselors of the National Cancer Institute and the Advisory Board of the Center on Immune Receptors at the Karolinska Institute in Stockholm, Sweden. He is currently a member of the Board of Management of the National Center for Biological Sciences in Bangalore, India; the Scientific Review Board of the Damon Runyon Cancer Research Foundation; and the Scientific Review Council of the Leukemia and Lymphoma Society. He also serves on the editorial board of multiple journals including Immunity, Molecular and Cellular Biology and the Journal of Biological Chemistry. He has published more than 100 articles.

Awards

2008 Frederick W. Alt Award for New Discoveries in Immunology Cancer Research Institute

Bibliography

Publications

Shim, J.H., et al. CHMP5 is essential for late endosome function and down-regulation of receptor signalling during mouse embryogenesis. J Cell Biol. 2006 Mar 27.

Shim, J.H., et al. TAK1, but not TAB1 or TA B2, plays an essential role in multiple signalling pathways in vivo. Genes Dev. 2005 Nov 15

Jimi, E. and S. Ghosh. Role of nuclear factor-kappaB in the immune system and bone. Immunol Rev. 2005 Dec.

Jimi, E. et al. Activation of NF-{kappa}B promo tes the transition of large, CD43+ pre-B cells to small, CD43- pre-B cells. Int Immunol. 20 May 2005

Bailey ST, Ghosh S. 'PPAR'ting ways with inflammation. Nat Immunol., 2005 Oct 6

E. C. Ziegler, S. Ghosh, Regulating Inducible Transcription Through Controlled Localization. Sci. STKE 2005, re6 (2005).

di Meglio, P., A. Ianaro, and S. Ghosh, Amelioration of acute inflammation by systemic administration of a cell-permeable peptide inhibitor of NF-kappaB activation. Arthritis Rheum, 2005. 52(3): p. 951-8.

Lee, K.Y., et al., PDK1 nucleates T cell receptor-induced signalling complex for NF-kappaB activation. Science, 2005. 308(5718): p. 114-8.

Hayden, M.S. and S. Ghosh, Signaling to NF-kappaB. Genes Dev, 2004. 18(18): p. 2195-224.

Zhang, D., et al., A toll-like receptor that prevents infection by uropathogenic bacteria. Science, 2004. 303(5663): p. 1522-6.

Jimi, E., et al., Selective inhibition of NF-kappa B blocks osteoclastogenesis and prevents inflammatory bone destruction in vivo. Nat Med, 2004. 10(6): p. 617-24.

Marienfeld, R., et al., RelB forms transcriptionally inactive complexes with RelA/p65. J Biol Chem, 2003. 278(22): p. 19852-60.

Ma, X.Y., et al., The interferon-inducible p202a protein modulates NF-kappaB activity by inhibiting the binding to DNA of p50/p65 heterodimers and p65 homodimers while enhancing the binding of p50 homodimers. J Biol Chem, 2003. 278(25): p. 23008-19.

Wu, C. and S. Ghosh, Differential phosphorylation of the signal-responsive domain of I kappa B alpha and I kappa B beta by I kappa B kinases. J Biol Chem, 2003. 278(34): p. 31980-7.

May, M.J., R.B. Marienfeld, and S. Ghosh, Characterization of the Ikappa B-kinase NEMO binding domain. J Biol Chem, 2002. 277(48): p. 45992-6000.

Zhang, G. and S. Ghosh, Negative regulation of toll-like receptor-mediated signalling by Tollip. J Biol Chem, 2002. 277(9): p. 7059-65.

Zhong, H., et al., The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. Mol Cell, 2002. 9(3): p. 625-36.

D'Acquisto, F., M.J. May, and S. Ghosh, Inhibition of Nuclear Factor Kappa B (NF-B):: An Emerging Theme in Anti-Inflammatory Therapies. Mol Interv, 2002. 2(1): p. 22–35.

Budde, L.M., et al., Regulation of IkappaBbeta expression in testis. Mol Biol Cell, 2002. 13(12): p. 4179-94.

Ghosh, S. and M. Karin, Missing pieces in the NF-kappaB puzzle. Cell, 2002. 109 Suppl: p. S81-96.

D'Acquisto, F. and S. Ghosh, PACT and PKR: turning on NF-kappa B in the absence of virus. Sci STKE, 200 1. 2001(89): p. RE1.

Zhang, G. and S. Ghosh, Toll-like receptor-mediated NF-kappaB activation: a phylogenetically conserved paradigm in innate immunity. J Clin Invest, 2001. 107(1): p. 13-9.

May, M.J., et al., Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science, 2000. 289(5484): p. 1550-4.

Voll, R.E., et al., NF-kappa B activation by the pre-T cell receptor serves as a selective survival signal in T lymphocyte development. Immunity, 2000. 13(5): p. 677-89.

Millet, I., et al., Inhibition of NF-kappaB activity and enhancement of apoptosis by the neuropeptide calcitonin gene-related peptide. J Biol Chem, 2000. 275(20): p. 15114-21.

Li, B., et al., Role of the guanosine triphosphatase Rac2 in T helper 1 cell differentiation. Science, 2000. 288(5474): p. 2219-22.

Fenwick, C., et al., A subclass of Ras proteins that regulate the degradation of IkappaB. Science, 2000. 287(5454): p. 869-73.

Budde, L.M. and S. Ghosh, Cloning and characterisation of the gene encoding mouse IkappaBbeta. Gene, 2000. 247(1–2): p. 279-86.

Zhang, G. and S. Ghosh, Molecular mechanisms of NF-kappaB activation induced by bacterial lipopolysaccharide through Toll-like receptors. J Endotoxin Res, 2000. 6(6): p. 453-7.

Wu, C. and S. Ghosh, beta-TrCP mediates the signal-induced ubiquitination of IkappaBbeta. J Biol Chem, 1999. 274(42): p. 29591-4.

Kopp, E., et al., ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev, 1999. 13(16): p. 2059–71.

May, M.J. and S. Ghosh, IkappaB kinases: kinsmen with different crafts. Science, 1999. 284(5412): p. 271-3.

Ghosh, S., Regulation of inducible gene expression by the transcription fact or NF-kappaB. Immunol Res, 1999. 19(2–3): p. 183-9.

Voll, R.E. and S. Ghosh, Role of NF-kappa B in T-lymphocyte development. Cold Spring Harb Symp Quant Biol, 1999. 64: p. 485-90.

May, M.J. and S. Ghosh, Signal transduction through NF-kappa B. Immunol T oday, 1998. 19(2): p. 80-8.

Medzhitov, R., et al., MyD88 is an adaptor protein in the hToll/IL-1 receptor family signalling pathways. Mol Cell, 1998. 2(2): p. 253-8.

Zhong, H., R.E. Voll, and S. Ghosh, Phosphorylation of NF-kappa B p65 by PKA stimula tes transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell, 1998. 1(5): p. 661-71.

Ghosh, S., M.J. May, and E.B. Kopp, NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol, 1998. 16: p. 225-60.

Zhong, H., et al., The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell, 1997. 89(3): p. 413-24.

Phillips, R.J. and S. Ghosh, Regulation of IkappaB beta in WEHI 231 mature B cells. Mol Cell Biol, 1997. 17(8): p. 4390-6.

May, M.J. and S. Ghosh, Rel/NF-kappa B and I kappa B proteins: an overview. Semin Cancer Biol, 1997. 8(2): p. 63–73.

Suyang, H., et al., Role of un phosphorylated, newly synthesised I kappa B beta in persistent activation of NF-kappa B. Mol Cell Biol, 1996. 16(10): p. 5444-9.

Johnson, D.R., et al., A sustained reduction in IkappaB-beta may contribute to persistent NF-kappaB activation in human e ndothelial cells. J Biol Chem, 1996. 271(27): p. 16317-22.

Phillips, R.J., S. Gustafson, and S. Ghosh, Identification of a novel NF-kappaB p50-related protein in B lymphocytes. Mol Cell Biol, 1996. 16(12): p. 7089-97.

Ghosh, G., et al., Structure of NF-kappa B p50 homodimer bound to a kappa B site. Nature, 1995. 373(6512): p. 303-10.

Thompson, J.E., et al., I kappa B-beta regulates the persistent response in a biphasic activation of NF-kappa B. Cell, 1995. 80(4): p. 573-82.

Kopp, E.B. and S. G hosh, NF-kappa B and rel proteins in innate immunity. Adv Immunol, 1995. 58: p. 1–27.

Kopp, E. and S. Ghosh, Inhibition of NF-kappa B by sodium salicylate and aspirin. Science, 1994. 265(5174): p. 956-9.

Ghosh, S., et al., Cloning of the p50 DNA bin ding subunit of NF-kappa B: homology to rel and dorsal. Cell, 1990. 62(5): p. 1019–29.

Ghosh, S. and D. Baltimore, Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature, 1990. 344(6267): p. 678-82.

References

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