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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

Proteostasis and Disease Regulation

Protein metabolism is essential for normal cellular function and it involves synthesis, folding, transport and degradation of proteins in a cell on a constant basis. Chaperones post-translationally promote newly synthesized proteins into a correctly folded functional protein. Protein translocation machinery, proteasome and autophagy processes are the critical events for protein subcellular localization and degradation. Stress as well as aging confronts chaperone function and protein clearance network that lead to protein misfolding, protein overload and cellular dysfunction. In human protein misfolding, aggregation and impaired protein clearance mechanism are the features of many neurodegenerative diseases, cancer and metabolic diseases.

The aim of our research is to delineate the mechanism of protein misfolding, aggregation and protein quality control system in cancer and neurodegenerative diseases. We use multi-disciplinary approaches combining biochemistry, biophysics, animal model, advanced microscopy and mass spectrometry-based proteomics to address our research questions.

Current research project:

  • Post-translational modification of proteins
    Protein post-translational modification (PTM), one of the important mechanisms, contributes enormous functional diversity in the proteome and governs many cellular processes. Primary, secondary and tertiary structures of a protein dictate its structural fold. However, a function of a protein is often determined by PTMs that provide the specificity, stability and localization. More than 250 PTMs have been identified but only a few of them are being studied. The progress of mass spectrometry-based proteomics enables us to identify and quantify PTMs and unravel the mechanism of how multiple PTM signals are integrated at cellular and organism level. Our group aims to investigate the qualitative and quantitative change of PTMs like ubiquitination, phosphorylation, redox-modification, acetylation and glycosylation in disease condition particularly cancer and neurodegenerative diseases.
  • Deubiquitinating enzymes and disease regulation
    One of the important aspects of our research is to understand the ubiquitin signaling mechanisms and their regulation in different diseases. Human genome analysis and proteomics data reveal almost one hundred deubiquitinating enzymes (DUBs), which majorly regulate ubiquitin homeostasis in cells. However, molecular functions of most of the DUBs are still elusive. We are investigating the molecular basis of their involvement in cellular functions like protein degradation, histone modification and endocytosis of plasma membrane proteins. It has also been revealed that the dysregulation of deubiquitinating enzymes leads to diseases like cancer and neurodegeneration. Our aim is to understand the possible molecular mechanisms underlying these diseases.
  • Protein aggregation mechanism in neurodegenerative diseases
    Neurodegenerative diseases are characterized by progressive loss of structure and function of neurons in the specific brain region. The hallmark of these disease pathogenesis is often associated with the abnormal accumulation of intracellular or extracellular protein aggregates that are characteristic for each disease. Neurodegenerative diseases are often considered as a conformational disorder. Increasing evidence suggests that genetic mutations or environmental factors can induce protein misfolding and aggregation in these diseases. The impairment of the protein quality control leads to the abnormal accumulation of disease-specific proteins. Here we aim to understand the mechanism of protein aggregation and its toxicity that contribute to disease outcome.

Maternal and Infant Health

Preterm birth is one of the major global public health problems and it is the single largest cause of neonatal deaths. India contributes the highest number of preterm birth and deaths worldwide (~25%). From a clinical perspective, it is of paramount importance to understand the molecular processes involved in preterm birth for early prediction, or prevention of preterm birth. RCB partners with THSTI, NIBMG and other institutions in embarking upon an Inter-Institutional program on preterm birth.

Our group is leading mass spectrometry based proteomics of preterm birth project. We are investigating the proteomics alterations that occur at different stages of pregnancy to identify the proteins that are altered in preterm birth and molecular pathways that are altered in relation to preterm birth. The long-term goal of this project is to identify the biomarkers relevant for early prediction of preterm birth or future target molecule for drug discovery.

Current research project:

  • Mass spectrometry based quantitative proteomics for early prediction of preterm birth.
  • Stress outcomes on pregnancy, fetal growth and birth weight: Development of methods to identify mothers at risk of preterm birth and intrauterine growth restriction resulting from maternal stress.
    • 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
    • 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
    • Dr. Sharad Vashisth
      Research Associate
    • Himani Joshi
      Junior Research Fellow
    • Sandhini Saha
      Junior Research Fellow
      sandhini@rcb.res.in
  1. Kumar R, Kumari R, Kumar S, Jangir DK, Maiti TK. (2018) Extracellular α-synuclein disrupts membrane nanostructure and promotes S-nitrosylation induced neuronal cell death. Biomacromolecules [Epub ahead of print]
  2. Kumar S, Jangir DK, Kumar R, Kumari M, Bhavesh NS, Maiti TK. (2018) Role of Sporadic Parkinson Disease Associated Mutations A18T and A29S in Enhanced α-Synuclein Fibrillation and Cytotoxicity. ACS Chem Neurosci 9:240
  3. Kumar P, Bag S, Ghosh TS, Dey P, Dayal M, Saha B, Verma J, Pant A, Saxena S, Desigamani A, Rana P, Kumar D, Sharma NC, Hanpude P, Maiti TK, Mukhopadhyay AK, Bhadra RK, Nair GB, Ramamurthy T, Das B. (2018) Molecular Insights into Antimicrobial Resistance Traits of Multidrug Resistant Enteric Pathogens isolated from India. Sci Rep 7:14468
  4. Hanpude P, Bhattacharya S, Singh AK, Maiti TK. (2017) Ubiquitin Recognition of BAP1: Understanding its Enzymatic Function. Biosci Rep 37
  5. Mukherjee S, Mukherjee S, Maiti TK, Bhattacharya S, Sinha Babu SP (2017) A Novel Ligand of Toll-like Receptor 4 From the Sheath of Wuchereria bancrofti Microfilaria Induces Proinflammatory Response in Macrophages. J Infect Dis 215:954
  6. Kumar R, Jangir KD, Verma G, Shekhar S, Hanpude P, Kumar S, Kumari R, Singh N, Sarovar NB, Ranjan NJ, Maiti TK (2017) S-nitrosylation of UCHL1 induces its structural instability and promotes α-synuclein aggregation. Sci Rep 7:44558
  7. Mukherjee S1, Chattopadhyay M1, Bhattacharya S2, Dasgupta S3, Hussain S4, Bharadwaj SK4, Talukdar D4, Usmani A, Pradhan BS, Majumdar SS, Chattopadhyay P, Mukhopadhyay S, Maity TK, Chaudhuri MK, Bhattacharya S (2017) A Small Insulinomimetic Molecule Also Improves Insulin Sensitivity in Diabetic Mice. PLoS One 12:e0169809
  8. 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
  9. Hanpude P, Bhattacharya S, Dey AK, Maiti TK (2015)  Deubiquitinating enzymes in cellular signaling and disease regulation. IUBMB Life 67:544.
  10. Maiti TK, Yamada K, Inoue K, Kandori H. (2012) L105K Mutant of Proteorhodopsin. Biochemistry 51:3198.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. Ghosh KS, Maiti TK, Debnath J, Dasgupta S. (2007) Inhibition of Ribonuclease A by polyphenols present in green tea. Proteins 69:566.
  17. Chatterjee J, Maiti TK, Dasgupta S. (2006) Isolation and partial characterization of ribonuclease inhibitor from goat liver. Protein Pept Lett 13:779.
  18. 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.
  19. 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.
  20. 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.
  21. 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.
  22. 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.
  23. 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.
  24. Ghosh KS, Maiti TK, Dasgupta S. (2004) Green tea polyphenols as inhibitors of ribonuclease A. Biochem Biophys Res Commun 325:807.
  25. 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.
  26. 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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