Building
Digital India

Dr. Tushar K Maiti

Associate Professor
E-mail: tkmaiti at rcb dot res dot in

  • Postdoc at Nagoya Institute of Technology (Japan), Purdue University (USA),
    and Weizmann Institute of Science (Israel)
  • PhD 2005, Indian Institute of Technology
  • Associate Professor

Ubiquitin mediated signaling in cellular processes

Protein metabolism is essential for normal cellular function and involves both synthesis and degradation of proteins on a constant basis. Eukaryotic cells are equipped with three different systems to accomplish protein degradation: mitochondrial proteases, which degrade the majority of mitochondrial proteins, lysosomes, which degrade membrane and endocytosed proteins, and the ubiquitin-proteasome system, which degrades the vast majority of long and short-lived normal and abnormal intracellular proteins. In fact, up to 80-90% of all intracellular proteins are degraded via the ubiquitin-proteasome system, which is considered to be the major pathway of intracellular protein degradation. A wide variety of biological processes are controlled by the reversible, post-translational modification of proteins, which is a covalent attachment of ubiquitin, a highly conserved 76-residue polypeptide. Like protein phosphorylation, the ubiquitin-proteasome system is a dynamic and reversible process, involving enzymes that add ubiquitin (E1 activating enzymes, E2 conjugating enzymes and E3 ligases) and enzymes that remove ubiquitin (deubiquitinating enzymes or DUBs).

The main focus of our laboratory is to understand the ubiquitin-proteasome signaling system, which regulates different cellular process like cell cycle progression, proliferation, differentiation, transcriptional activation and signal transduction. Besides normal function, the ubiquitin proteasome system (USP) contributes to several pathological states of clinical disorder including inflammation, neurological disorder and cancer by altering the function of activating, conjugating, ligating and deubiqutinating enzymes. Understanding the molecular basis for function of ubiquitin pathway enzymes will provide a better understanding of ubiquitin signaling system and helps in therapeutic intervention of UPS related diseases. Our approach studying the ubiquitin proteasome system is based on the combined application of biochemistry, biophysics, structural biology, mass spectrometry-based proteomics and chemical biology.

    • Amit Kumar Dey
      Research Associate
    • Pranita Hanpude
      Senior Research Fellow
      pranita@rcb.ac.in
    • Roshan Kumar
      Senior Research Fellow
      roshankumar602@gmail.com
    • Tanu Johari
      Senior Research Fellow
      tanu.johari@rcb.res.in
    • Sanjay Kumar
      Senior Research Fellow
      sanjay.kumar@rcb.res.in
    • Raniki Kumari
      Senior Research Fellow
      raniki@rcb.res.in
    • Neha Sharma
      Project Assistant
      nehasharma@rcb.res.in
    • Manisha Kumari
      Junior Research Fellow
      Manisha.kumari@rcb.res.in
    • Abhisekh Kumar Singh
      Senior Research Fellow (Project)
      abhisheksingh@rcb.res.in
    • Bhoj Kumar
      Research Associate
      Bhoj.kumar@rcb.res.in
    • Tuhin Subha Haldar
      Junior Research Fellow
      tuhin@rcb.res.in
    • Bharat Singh
      Young Investigator
      bharat.singh@rcb.res.in
    • Sandhini Saha
      Junior Research Fellow
      sandhini@rcb.res.in
    • Deepali Chhoker
      Project Assistant
      deepali@rcb.res.in
    • Saibal Saha
      Junior Research Fellow
      saibal@rcb.res.in
    • Sreenath Kancham
      Junior Research Fellow
      sreenath.kanchan@rcb.res.in
    • Nazia Rifat Zaman
      Research Fellow
      nazia@rcb.res.in
  1. Bhattacharya S, Hanpude P, Maiti TK. (2015)  Cancer associated missense mutations in BAP1 catalytic domain induce amyloidogenic aggregation: A new insight in enzymatic inactivation. Sci Rep 5:18462
  2. Hanpude P, Bhattacharya S, Dey AK, Maiti TK (2015)  Deubiquitinating enzymes in cellular signaling and disease regulation. IUBMB Life 67:544.
  3. Maiti TK, Yamada K, Inoue K, Kandori H. (2012) L105K Mutant of Proteorhodopsin. Biochemistry 51:3198.
  4. Boudreaux D, Chaney J, Maiti TK, Das C. (2012) Contribution of active site glutamine to rate enhancement in ubiquitin C-terminal hydrolases. FEBS J 279:1106.
  5. Maiti TK, Permaul M, Mahanic C, Mauney S, Das C. (2011) Crystal Structure of Catalytic Domain of UCHL5, a Proteasome Associated Deubiquitinase, Reveals an Auto-Inhibited Conformation of the Enzyme. FEBS J 278:4917.
  6. Boudreaux D, Maiti TK, Davies CW, Das C. (2010) Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation. Proc Natl Acad Sci USA. 107:9117.
  7. Maiti TK, Engelhard M, Sheves M. (2009) Retinal-Protein interactions in Halorhodopsin from Natronomonas pharaonis: Binding and Retinal thermal Isomerization catalysis. J Mol Biol 394:472.
  8. Maiti TK, Ghosh KS, Samanta A, Dasgupta S. (2008) The interaction of Silibinin with Human serum albumin: A spectroscopic investigation. J Photochem Photobiol A 194:297.
  9. Ghosh KS, Maiti TK, Debnath J, Dasgupta S. (2007) Inhibition of Ribonuclease A by polyphenols present in green tea. Proteins 69:566.
  10. Chatterjee J, Maiti TK, Dasgupta S. (2006) Isolation and partial characterization of ribonuclease inhibitor from goat liver. Protein Pept Lett 13:779.
  11. Sardar PS, Maity SS, Ghosh S, Chatterjee J, Maiti TK, Dasgupta S. (2006) Characterization of the tryptophan residues of human placental ribonuclease inhibitor and its complex with bovine pancreatic ribonuclease A by steady-state and time-resolved emission spectroscopy. J Phys Chem B 110:21349.
  12. Ghosh KS, Maiti TK, Mandal A, Dasgupta S. (2006) Copper complexes of (-) epicatechin gallate and (-)-epigallocatechin gallate act as inhibitors of Ribonuclease A. FEBS Lett 580:4703.
  13. Leonidas DD, Maiti TK, Samanta A, Dasgupta S, Pathak T, Zographos SE, Oikonomakos NG. (2006) The binding of 3'-N-piperidine-4-carboxyl-3'-deoxy-ara-uridine to ribonuclease A in the crystal. Bioorg Med Chem 14:6055.
  14. Maiti TK, Ghosh KS, Dasgupta S. (2006) Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: fluorescence, fourier transform infrared, circular dichroism, and docking studies. Proteins 64:355.
  15. Maiti TK, Ghosh KS, Debnath J, Dasgupta S. (2006) Binding of all-trans retinoic acid to human serum albumin: fluorescence, FT-IR and circular dichroism studies. Int J Biol Macromol 38:197.
  16. Maiti TK, De S, Dasgupta S, Pathak T. (2006) 3'-N-Alkylamino-3'-deoxy-ara-uridines: a new class of potential inhibitors of ribonuclease A and angiogenin. Bioorg Med Chem 14:1221.
  17. Ghosh KS, Maiti TK, Dasgupta S. (2004) Green tea polyphenols as inhibitors of ribonuclease A. Biochem Biophys Res Commun 325:807.
  18. Maiti TK, Chatterjee J, Dasgupta S. (2003) Effect of green tea polyphenols on angiogenesis induced by an angiogenin-like protein. Biochem Biophys Res Commun 308:64.
  19. Maiti TK, Dasgupta S. (2002) Isolation and characterization of an angiogenin-like protein from goat plasma. Protein Pept Lett 9:283.

Dr. Tushar K Maiti
Associate Professor
Regional Centre for Biotechnology
NCR Biotech Science Cluster
3rd Milestone, Faridabad-Gurgaon Expressway
P.O. Box No. 3, Faridabad - 121 001
Haryana (NCR Delhi), India
E-mail: tkmaiti at rcb dot res dot in
Phone: 91 129-2848826

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