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Dr. MANAS KUMAR SANTRA

Scientist 'D'
National Centre for Cell Science
NCCS Complex, Pune University Campus
Ganeshkhind, PUNE- 411 007, INDIA
Ph.: +91-020-25708150, 25708000
Fax: +91-020-25692259
E-mail:

Education and Experience | Area of Research | Publications |Awards | Memberships | Lab Members

 

 

Education and Experience

  • 2010 to present: Scientist D, National Centre for Cell Science, Pune, India.

  • 2006 - 2010: Postdoctoral Fellow, University of Massachusetts Medical School, USA

  • 2001 - 2006: Ph. D., Indian Institute of Technology Bombay

  • 1999 - 2001: M. Tech. (2001), Indian Institute of Technology Bombay

  • 1996 - 1998: M. Sc. (Chemistry), Vidyasagar University, West Bengal

  • 1996: B. Sc. (Chemistry), Bajkul Milani Mahavidyalaya, Vidyasagar University, West Bengal

 

 

 

Area of Research

 

Gene Regulation by SCF-E3 Ubiquitin Ligase:

 

Ubiquitin ligases are specific class of proteins mainly contributing to the proteasomal degradation of many key proteins involved in the cell cycle regulation as well as many signalling pathways. These are well suited to regulate molecular networks that operate at post-translational level. SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes are best studied E3 ubiquitin ligase. The F-box proteins act as a substrate receptor and determine the substrate specificity for the complex. Deregulation of this proteolytic system might result in uncontrolled proliferation, genomic instability and diseases like cancer. Although there are 69 F-box genes present in the human genome, majority of them remain uncharacterized. The inherent interacting capability of these proteins makes them important regulators of various important cellular processes like cell cycle progression, apoptosis, senescence, metabolism etc. Our lab is interested in identifying the F-box proteins having potential role in tumor biology and elucidating their molecular mechanism through different molecular cell biology, biochemistry and proteomic approaches.

 

Fig1

Schematic representation of SCF E3 ubiquitin ligase function

 

 

 

Epigenetic Regulation of Gene Expression:

Understanding the Role of Epigenetic Gene Regulation in Cancer:

 

Epigenetics is the study of heritable changes in gene expression without altering the DNA sequence. Along with the genetic, epigenetic mechanism of gene regulation plays an important role in tissue specific spatio-temporal gene expression pattern, perturbation of which leads to diseases like cancer. Cancer arises due to the inactivation of the tumor suppressor genes and activation of oncogenes. In many instances, loss of function of tumor suppressor genes is due to epigenetic alterations.  
Our lab is interested in deciphering how and why the tumor suppressor genes are epigenetically silenced in cancer through the use of RNAi tools.

 

Fig2

Schematic representation of epigenetic regulation of gene expression

 

 

Understanding Epigenetic mechanisms regulating pancreatic β-cell Development:

 

While the eukaryotic genome is the same throughout all somatic cells in an organism, there are specific structures and functions that discern one type of cell from another. These differences are due to the cell’s unique gene expression patterns that are determined during cellular differentiation. Emerging evidences have shown that epigenetics plays a central role in cellular differentiation. Pax4 is a very important transcription factor highly expressed in the developing pancreatic β-cells in the early stages; however, it is silenced in mature β-cells.
We are interested in dissecting the epigenetic mechanisms underlying Pax4 silencing, thereby regulating pancreatic β-cell development, through various in vitro and in vivo studies.

 

Identification and elucidation of the role of Protein Phosphatase 1 regulatory subunits in Cancer:

Proteins are the functional unit of a cell and post translational modifications (PTMs) dictate their cellular functions. Among the different PTMs, phosphorylation (mediated by kinases) and dephosohorylation (carried out by phosphatases) are the most important one. The phosphatases are key players in maintaining normal cellular homeostasis, as illustrated by the dephosphorylation of p53 to bring down the cell to normal steady state after DNA damage response. There are many protein phosphatases (PP) in the cell, namely PP1, PP2, PP4, PP5, PP6 etc. Protein phosphatase 1 (PP1) belongs to the family of serine-threonine phosphatases and forms a major fraction of the cellular phosphatase pool. It plays significant roles in almost all important cellular functions such as cell cycle regulation, stress response and many more. Differential recruitment of regulatory subunits of PP1 dictates the substrate specificity for its function.
Taking into consideration the significance of PP1 in cellular functions, our lab is interested in exploring the repertoire of PP1 regulatory subunits having a role in cancer biology.


 

 

 

Publications

  1. Kumar, P., Gorai, S., Santra, M. K., Mondal, B. and Manna, D. (2012) DNA binding, nuclease activity and cytotoxicity studies of Cu (II) complexes of tridentate ligands. Dalton Trans. 41, 7573-7581.

  2. Santra, M. K., Wajapeyee, N. and Green, M. R. (2009) F-Box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest following DNA damage, Nature, 459, 722-725.

  3. Palakurty, R., Wajapeyee, N., Santra, M. K., Ling, L., Gazin, C, Gobeil, S. and Green, M. R. (2009) Epigenetic silencing of RASSF1A tumor suppressor gene through HOXB3-mediated induction of DNMT3b expression. Molecular Cell 36, 219-230.

  4. Welch, C., Santra, M. K., Zhu, X., El-Assaad, W., Huber, W. E., Keys, R. A., Jose, G. Teodoro, J. G. and Green, M. R. (2009) Identification of a protein, G0S2, that lacks Bcl-2 homology domains and interacts with and antagonizes Bcl-2. Cancer Research,69, 6782-6789.

  5. Hart, D. Santra, M. K. and Green, M. R. (2009) Selective interaction of TAF3 and TRF3 regulates the embryonic development. Developmental Dynamics, 238, 2540-2549.

  6. Santra, M, K. and Panda, D. (2007) Acid-induced loss of functional properties of bacterial cell division protein FtsZ: evidence for an alternative conformation at acidic pH. Proteins 67, 177 - 188.

  7. Beuria, T. K., Shah, J. H., Santra, M. K., Kumar, V. and Panda, D. (2006) Effects of pH and ionic on the assembly and bundling of FtsZ protofilaments: a possible role of electrostatic interactions in the bundling of protofilaments. Int. J. Biol. Macromol. 40, 30 - 39.

  8. Santra, M. K., Dasgupta, D. and Panda, D. (2006) Pyrene Excimer Fluorescence of Yeast Alcohol Dehydrogenase: A Sensitive Probe to Investigate Ligand Binding and Unfolding Pathway of the Enzyme. Photochem. Photobiol. 82, 480 - 486.

  9. Santra, M. K., Dasgupta, D. and Panda, D. (2005) Deuterium oxide promotes assembly and bundling of FtsZ protofilaments. Proteins 61, 1101-1110

  10. Panda, D., Rathinasamy, K., Santra, M. K. and Wilson, L. (2005) Kinetic suppression of microtubule dynamic instability by griseofulvin: implications for its possible use in the treatment of cancer. Proc. Natl. Acad. Sci. USA 102, 9878-9883

  11. Beuria, T. K., Santra, M. K. and Panda, D. (2005) Sanguinarine Blocks Cytokinesis in Bacteria by Inhibiting FtsZ Assembly and Bundling. Biochemistry 44, 16584-16593

  12. Santra, M. K., Banerjee, A., Rahaman, O. and Panda, D. (2005) Unfolding pathways of human serum albumin: Evidence for sequential unfolding and folding of its three domains. Int. J. Biol. Macromol. 37, 200-204

  13. Mukherjee, A., Santra, M. K., Beuria, T. K. and Panda, D. (2005) A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea. FEBS J. 272, 2760-2772

  14. Santra, M. K., Banerjee, A., Krishnakumar, S. S., Rahaman, O. and Panda, D. (2004) Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding. Eur J. Biochem. 271, 1789-1797

  15. Santra, M. K., Beuria, T. K., Banerjee, A. and Panda, D. (2004) Ruthenium red-induced bundling of bacterial cell division protein, FtsZ.J. Biol. Chem. 279, 25959-25965

  16. Santra, M. K. and Panda, D. (2003) Detection of an intermediate during unfolding of bacterial cell division protein FtsZ: loss of functional properties precedes the global unfolding of FtsZ. J. Biol. Chem. 278, 21336-21243

 

Awards

  • Charles A. King Trust Postdoctoral Research Fellowship Award, USA (2010 )

  • Ramalingaswami Fellowship from Department of Biotechnology, Govt. of India (2010)

  • Innovative Young Biotechnologist Award from Department of Biotechnology, Govt. of India (2008)

  • Young Scientist Award in New Biology from Indian Science Congress Association (2006)

  • Best research scholar award from IIT Bombay (2006)

 

Memberships

  • Life member for the Society of Biological Chemists

  • Life member for Indian Association for Cancer Research

  • Life Member of Indian Science Congress Association

 

Lab Members

 

Ph.D. Students
ParulDatta

Parul Datta
Ph.d Student (UGC-JRF)
paruldutta5@gmail.com

Srinadh

Srinadh Choppara
Ph.D student (CSIR-JRF)
srinadhchoppara@gmail.com

   
Rajesh

Rajesh K.M.
Ph.D student (UGC-JRF)
rkmanne@nccs.res.in

Sachin

Sachin N. M. Meshram
Ph.D. Student (CSIR-JRF)
sachin10meshram@gmail.com

   
Post Doctoral Fellow
Avinash

Avinash Kumar
DBT-Post Doctoral Fellow
avinashk@nccs.res.in

 
   
Project Staff

Asha Patel
Project -JRF
ashapatel931@gmail.com

   
Lab Alumni
Bhargav

Bhargav Waghela
(2011-12)
wbhargav@gmail.com

Lakshmana

Lakshmana Kumar Kasarapu
(2011-12)
lnkumar2012@gmail.com

 

 

 

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NCCS Complex,University of Pune Campus,Ganeshkhind,Pune 411007,Maharashtra,India Phone: +91-20-25708000 Fax:+91-20-25692259 Gram:ATCELL