Molecular Biologist with experience in Signal Transduction looking for a suitable position

Raghu K. Chari raghuk at
Sat Jun 24 20:25:06 EST 1995

  Looking for a suitable position (Industry/Academia)

  1. Ph.D. with 6 years of postdoctoral experience

  2. Experience in Signal Transduction and Immunology

  3. Refer to the attached CV for details

  4. E-Mail reply can be mailed to raghuk at


  G. Panchamoorthy, Ph.D.

                                 Curriculum Vitae

Name:             Govindaswamy Panchamoorthy

Address:          1575 Tremont Street, Apt # 901, Boston, MA 02120
                  Phone: 617-566-0355 (home);     617-432-4979 (work)

Visa Status:      Permanent Resident


    1989 Ph.D.    Biochemistry - All India Institute of Medical Sciences, New Delhi,
    1982 M.Sc.    Life Sciences - Jawaharlal Nehru University, New Delhi, India.
    1980 B.Sc.    Chemistry - University of Madras, India.

Postdoctoral Training:

    Research Fellowships:

    1992-present  Research Fellow, Lymphocyte Biology Section, Brigham and
                  Women's Hospital, Harvard Medical School, Boston, MA
    1990-1992     Research Fellow, Laboratory of Immunochemistry, Dana-Farber
                  Cancer Institute, Harvard Medical School, Boston, MA
    1988-1989     Research Associateship from Department of Science and
                  Technology, Government of India, New Delhi

Awards and Honors:

    1993-1995     Research fellowship award from The Medical Foundation/Charles
                  A. King Trust, Boston, MA.
    1982-1988     Junior Research Fellowship from Indian Council of Medical
    1980-1982     Merit Scholarship from Jawaharlal Nehru University, New Delhi,
    1976-1980     Government of India National Merit Loan Scholarship


    1993-present  American Association for the Advancement of Science
    1983-1989     Indian Immunology Society
    1982-1989     Society of Young Scientists, New Delhi.

Teaching Experience:

    1983-1989     Taught theory and practicals in immunology and biochemistry for
                  medical (M.B.B.S) and undergraduate (Human Biology)
                  students, All India Institute of Medical Sciences, New Delhi,


Original Articles:

1.  Panchamoorthy G, Fukazawa T, Stolz L, Payne G, Reedquist K, Shoelson S,
    Songyang Z, Cantley L, Walsh C and Band H. Physical and functional
    interactions between SH2 and SH3 domains of the Src family protein tyrosine
    kinase p59fyn. Mol. Cell. Biol. 1994; 14: 6372.

2.  Reedquist K, Fukazawa T, Druker B, Panchamoorthy G, Shoelson s, and Band
    H. Rapid T-cell receptor-mediated tyrosine phosphorylation of p120, an Fyn/Lck
    Src homology 3 domain-binding protein. Proc. Natl. Acad. Sci. USA. 1994; 91:

3.  Fukazawa T, Reedquist K, Trub T, Soltof S, Panchamoorhty G, Druker B,
    Cantley L, Shoelson S, Band H.  SH3 domain binding T cells tyrosyl
    phosphoprotein p120: identity with c-cbl protoncogene product and in vivo
    complexes with Grb2 and PI3-kinase. (J. Biol. Chem. In press).

4.  Fukazawa T, Reedquist K, Panchamoorthy G, Soltoff S, Trub T, Druker B,
    Cantley L, Shoelson S, Band H.  T cell activation-dependent association between
    p85 subunit of the PI 3-kinase and Grb2/PLC 1-binding phosphotyrosyl protein
    pp36/38. (J. Biol. Chem., in press)

5.  Panchamoorthy G, McLean J, Modlin RL, Morita CT, Ishikawa S, Brenner MB,
    Band H.  A Predominance of the T Cell Receptor Vþ2/Vë2 Subset in Human
    Mycobacteria-Responsive T Cells Suggests Germline Gene Encoded Recognition. 
    J Immunol.  1991; 147:3360.

6.  Uyemura K, Deans RJ, Band H, Ohmen J, Panchamoorthy G, Morita CT, Rea
    TH, Modlin RL.  Evidence for clonal selection of þë T-cells in response to a
    human pathogen. J. Exp. Med. 1991; 174:683.

7.  Band H, Porcelli SA, Panchamoorthy G, McLean J, Morita CT, Ishikawa S,
    Modlin R, Brenner MB.  Antigens and antigen-presenting molecules for þë T
    cells.  Current Topics in Microbiology and Immunology.  1991; 173:229.

8.  Band H, Panchamoorthy G, McLean J, Morita CT, Ishikawa S, Modlin R, Brenner
    MB.  Recognition of mycobacterial antigens by þë T cells.  33rd Forum in
    Immunology on "þë T Cells", Lefranc, M-P, Bonneville M, eds.  Research in
    Immunology.  1990; 141:645.

9.  Panchamoorthy G, Tiwari SC, and Srivastava LM.  Inherited structural and
    quantitative polymorphisms of C3b receptor (CR1) in normals and patients with
    glomerular diseases.  Asian Pac J Allergy Immunol. 1993; 11:123.

10. Panchamoorthy G, Tewari SC, Bora NS, Srivastava LM.  Decreased expression
    of C3b receptor (CR1) on the erythrocytes of patients with acute
    glomerulonephritis.  Clin Chem Enzym Comms.  1990; 2:167.

11. Srivastava LM, Panchamoorthy G, Saibaba KSS.  Relevance of complement
    system in clinical biochemistry.  Proc Assoc Clin Biochem of India.  1989; 34.

12. Das N, Bora NS, Panchamoorthy G, Srivastava LM.  Circulating immune
    complexes in myocardial infarction.  Ind J Med Res.  1987; 86:74.

13. Fukazawa T, Panchamoorthy G, Shoelson S, and Band H. Phosphotyrosyl
    Peptide-sensitive Binding of a Non-Phosphotyrosyl Protein, pp32 to SH2 Domain
    of FynB Binding of a non-phosphotyrosyl polypeptide pp32 to Fyn SH2 domain.
    In preparation. 

14. Reedquist K, Fukazawa T, Panchamoorthy G, Druker B, Band H.  Stimulation
    through the T cell receptor induces p120cbl association with crk proteins.
    (Submitted to J. Biol. Chem.)

15. Panchamoorhty G, Fukazawa T, Soltoff S, Reedquist K, Cantley L, Band H. 
    p120cbl is a major tyrosine phosphorylation substrate upon triggering through
    B cell antigen receptor and forms in vivo complexes with multiple signalling
    proteins.  In preparation.

16. Panchamoorthy G, Reedquist K, David V, Reeves W, Anderson C and Band H.
    Ku, the regulatory subunit of DNA-dependent protein kinase, forms a multi-
    protein complex. In preparation.

Papers Presented in Symposia/Conferences:

1.  Panchamoorthy G, Srivastava N, Gupta SP, Srivastava LM.  Evaluation of
    complement (C3) inhibition in vitro by drugs used in management of bronchial
    asthma.  Proc 11th Ann Conf of Indian Immunol Soc.  Hyderabad, India, 1985.

2.  Panchamoorthy G, Bora NS, Srivastava LM.  Genetic polymorphism of C3b
    receptor (CR1) in Indian population.  Proc 6th Internatl Cong of Immunol. 
    Toronto, Canada. 1986.

3.  Das N, Bora NS, Panchamoorthy G, Kazmi S, Srivastava LM.  Circulating
    immune complex in myocardial infarction.  Proc 6th Internatl Cong of Immunol. 
    Toronto, Canada.  1986.

4.  Panchamoorthy G, Bora NS, Srivastava LM.  Erythrocyte C3b receptor (CR1)
    levels in normal Indian population.  Proc 14th Ann Conf of Indian Immunol Soc. 
    Srinagar, India. 1987.

5.  Srivastava LM, Tiwari SC, Panchamoorthy G, Bora NS.  Acquired deficiency of
    C3b receptor (CR1) in acute glomerulonephritis.  Proc 7th Internatl Cong in
    Immunol.  Berlin, FRG, 1989.

6.  Panchamoorthy G, Tiwari SC, Bora NS, Srivastava LM.  Structural
    polymorphisms of C3b receptor (CR1) in normal North Indian population and
    patients with renal diseases.  Proc 16th Ann Conf of Indian Immunol Soc.  1989.

7.  Morita CT, Band H, Panchamoorthy G, Brenner MB. A major subset of human
    þë T cells reactive to mycobacterium tuberculosis is not restricted by classical
    MHC molecules. J  Cellular Biochem Supplement 16D: 68. Presented at the
    Keystone Symposium on Antigen Presentation Functions of the MHC, March 1992.

8.  Wagner LE, Romzek NC, Panchamoorthy G, Band H, Holoshitz J. A heat shock
    protein-  derived peptide enhances anti-tumor cytolytic activity of human þë T
    cell clones. Presented at the Annual Symposium of American Federation of
    Clinical Research, November 1992.

Research Experience

    Lymphocyte signal transduction
    Antigen recognition by þë T cell receptor
    Complement system and complement receptor
    Biochemical characterization of autoantigen, Ku and associated proteins


    Cellular and Molecular Immunology and Immunochemistry
    Cell Biology and Biochemistry
    Molecular Biology/Genetic Engineering


    Hamid Band, M.D., Ph.D.
    Assistant Professor of Medicine
    Lymphocyte Biology Section
    Department of Rheumatology and Immunology
    Brigham and Women's Hospital
    Boston, MA 02115
    Telephone: 617-432-1557

    Michael B. Brenner, M.D.
    Chief, Lymphocyte Biology Section
    Department of Rheumatology and Immunology
    Brigham and Women's Hospital
    Boston, MA 02115
    Telephone: 617-432-0614

    Harout Dersimonian, Ph.D.
    Assistant Professor
    Transplantation Biology Research Center
    Massachusetts General Hospital
    MGH East, Bldg 149, Rm 9019
    Charlestown, MA 02129
    Telephone: 617-726-4362

    Anjana Rao, Ph.D.
    Associate Professor of pathology
    Division of Tumor Virology
    Dana-Farber Cancer Institute
    44 Binney Street
    Boston, MA 02115.
    Telephone: 617-375-8265

    Christina M. Parker, M.D.
    Assistant Professor of Medicine
    Department of Rheumatology and Immunology
    Brigham and Women's Hospital
    Boston, MA 02115
    Telephone: 617-432-4971

Current Research Projects:

Biochemical and functional characterization of a novel Fyn SH3 domain-binding

    My current research project is focussed on the understanding of molecular
events involved in T cell receptor mediated signalling which involves protein
tyrosine kinases. One of the earliest identifiable biochemical events in response to
stimulation through T cell receptor (TCR) is the tyrosine phosphorylation of cellular
proteins including the receptor components.  Two src-family tyrosine kinases p59fyn
(Fyn) and p56lck (Lck) have been shown to play important roles in T cell signalling.
Similar to other src-family  tyrosine kinases, Fyn and Lck possess an N-terminal
myristylation signal that is essential for membrane anchoring, followed by a unique
domain that mediates  binding to CD3 and þ chains or CD4/8.  This region is followed
by non-catalytic Src-homology (SH3 and 2) domains, a highly conserved tyrosine
kinase domain, and a C-terminal domain that carries a negative regulatory tyrosine
phosphorylation site. The SH2 domains bind tyrosine phosphorylated motifs and thus
participate in the formation of activated signalling complexes. The SH3 domains bind
proline-rich motifs and mediate phosphorylation independent protein-protein
interactions. I have shown that the SH2 and SH3 domains of the tyrosine kinase
physically interact with each other and play a regulatory role on T cell signalling
(Mol. Cell. Biol, 1994; 14:6372). Specific ligand binding to one domain influences the
other domain in terms of its binding to cellular target proteins which control the
effector functions of the cell in response to antigens. Thus, the interaction of SH2
and SH3 domains suggest a novel mechanism of regulating the enzymatic activity of
src kinases and their interaction with other proteins.

    Deletion of SH3 domain among src-family kinases reveals their transforming
potential, suggesting SH3 domain has a negative regulatory role. Thus,
identification and characterization cellular proteins that interact with SH3 domains
of src-family tyrosine kinases is likely to lead to significant insights into the role of
these proteins in T cell signal transduction and may reveal the mechanisms of their
oncogenic transformation.

    I have developed a novel method for screening þExlox expression library to clone
specific genes encoding proteins that bind to Fyn SH3 domain and may therefore be
involved in T cell signalling in response to foreign antigen. I have used bacterially
expressed Fyn SH3 domain as a fusion protein with GST as a probe to screen the
library. One cDNA clone was found repeatedly and the open reading frame cDNA
fragments have proline-rich motifs which are characteristic of SH3 domain binding
proteins. Search for sequence identity or homologous sequences from the database
did not provide any matching sequences suggesting that the cDNA
obtained from the library repesent a novel SH3 domain-binding protein.
I have raised
antibodies against these proteins by injecting rabbits with GST fusion
obtained from these partial cDNA clones.  Currently, I am trying to
isolate the full
length cDNA clones for these proteins and simultaneously characterize
these SH3
binding proteins using the antibodies.

Characterization of c-cbl protooncogene in lymphocyte signal
    We have previously identified p120 as a Fyn/Lck SH3 domain binding
which is tyrosine phosphorylated very early following TCR triggering
(Proc. Natl.
Acad. Sci. USA. 1994; 91: 4135).  Further, using direct protein
purification, amino
acid sequence analysis, reactivity with antibodies and 2D-gel analysis
we have
identified p120 as the human c-cbl protooncogene product (communicated
to Mol.
Cell. Biol.). p120cbl possesses a large proline-rich region with
multiple putative
SH3-binding motifs and this region is included in the deletion that
renders v-cbl
oncogenic. p120cbl forms in vivo complexes with three SH2/SH3
signalling proteins: Fyn, Grb2, and p85 subunit of PI3-kinase.
Currently we are
trying to delineate the receptor-mediated lymphocyte signalling
pathways involving
p120cbl and characterizing the role of p120cbl in oncogenesis.


More information about the Immuno mailing list