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Dr. Tushar K Maiti

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
  • 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.
    • Dr. Nitu Singh
      MK Bhan Fellow
      nitu.singh@rcb.res.in
    • Dr. Archana Prasad
      DBT-Research Associate
      archana.prasad@rcb.res.in
    • Ms. Manisha Kumari
      DST-Senior Research Fellow
      manisha@rcb.res.in
    • Sandhini Saha
      CSIR-Senior Research Fellow
      sandhini@rcb.res.in
    • Mr. Sushanta Majumder
      CSIR- SPM Senior Research Fellow
      sushanta.majumder@rcb.res.in
    • Mr. Krishna Singh Bisht
      DST-Senior Research Fellow
      krishna.singh@rcb.res.in
    • Mr. Naman Kharbanda
      CSIR-Junior Research Fellow
      naman.phd20@rcb.res.in
    • Ms. Swati Aggarwal
      CSIR-Junior Research Fellow
      swati.aggarwal@rcb.res.in
    • Mr. Ankit Biswas
      DBT-Junior Research Fellow
      ankit.biswas@rcb.res.in

     Lab Alumni


    Postdoctoral Fellow

    • Dr. Sushmita Bhattacharya, RCB Young Investigator (2012- 2015).
      Present position: Scientist B, ICMR-National Institute of Cholera and Enteric Diseases, Kolkata.
    • Dr. Deepak Kumar Jangir, ICMR Research Associate (2014- 2016)
      Present position: Postdoctoral Fellow, University of Minnesota, USA.
    • Dr. Bharat Singh, RCB Young Investigator ( 2016-2017)
    • Dr. Amit Kumar Dey, Project Research Associate (2014-2020).
      Present position: Scientist, Biocon Pvt Ltd
    • Dr. Sanghati Bhattacharya, Project Senior Technology Officer (2018- 2020).
      Present position: Research Associate, IIT Delhi
    • Dr. Bhoj Kumar, Project Research Associate (2015-2021).
      Present position: Research Scientist, University of Georgia USA.
    • Dr. Archana Pant, SERB-N-PDF (2021-2021)
      Present position: DST -Inspire Faculty, National Institute of Immunology, New Delhi.

    Ph.D. students

    • Dr. Pranita Hanpude (2012-2017).
      Present position: Postdoctoral Research Fellow, Rutgers University, USA
    • Dr. Roshan Kumar (2013-2018).
      Present position: Postdoctoral Research Fellow, University of Michigan, USA
    • Dr. Tanu Johari (2014-2019).
      Present position: Senior Analyst at UDG Healthcare PLC, India
    • Dr. Nazia Rifat Zaman (Visiting Ph.D. student from University of Dhaka, Bangladesh)
      Present Position: Assistant Professor, Primeasia University, Bangladesh
    • Dr. Sanjay Kumar (2014-2020).
      Present position: Postdoctoral Fellow, Mayo Clinic, Florida, USA
    • Dr. Raniki Kumari (2014-2021).
      Present position: Postdoctoral Fellow, Johns Hopkins University, USA

    Master and Project Fellows

    • Mr. Abhishek Kumar Singh, Project Senior Research Fellow (2014-2019)
    • Ms. Neha Sharma, Project Assistant (2014-2017)
    • Mr. Rajarshi Chaudhuri, Integrated MSc-Ph.D. student (2019-2020).
  1. Khurana H, Srivastava M, Chaudhary D, Gosain TP, Kumari R, Bean AC, Chugh S, Maiti TK, Stephens CE, Asthana S and Singh R (2021) Identification of diphenyl furan derivative via high through put and computational studies as ArgA inhibitor of Mycobacterium tuberculosis. Int J Biol Macromol 193:1845.
  2. Verma R, Saha S, Kumar S, Mani S, Maiti TK and Surjit M (2021) RNA-Protein Interaction Analysis of SARS-CoV2 5' and 3' Untranslated regions reveals a role of Lysosome-Associated Membrane Protein-2a during viral Infection. mSystems 6: e0064321.
  3. Kumar S, Kumar R, Kumari M, Kumari R, Saha S and Maiti TK (2021) Ellagic acid inhibits alpha synuclein aggregation at multiple sates and reduced it cytotoxicity. ACS Chem Neurosci 12:1919.
  4. Kumari R and Maiti TK (2021) Calpain-2 participates in the process of calpain-1 inactivation by Shinkai-Ouchi et al. Bioscience Reports 41: BS20203690.
  5. Srikanth S, Rizvi ZA, Pandey RP, Dalal R, Rathore DK, Kumar B, Pandey M, Kumar Y, Goel R, Maiti TK, Tiwari A, Johri AK, Pandey AK and Awasthi A (2021) Gefitinib results in robust host-directed immunity against Salmonella infection through proteo-metabolomic reprogramming. Front Immunol 12: 648710.
  6. Pani T, Rajput K, Kar A, Sharma H, Basak R, Medatwal N, Saha S, Dev G, Kumar S, Gupta S, Mukhopadhyay A, Malakar D, Maiti TK, Arimbasseri AG, Deo SVS, Sharma RD, Bajaj A, and Dasgupta U (2021) Alternative splicing of ceramide synthase 2 alters levels of specific ceramides and modulates cancer cell proliferation and migration in Luminal B breast cancer subtype. Cell Death Dis 12:171.
  7. Kumar B, Dey AK, Saha S, Singh AK, Kshetrapal P, Wadhwa N, Thiruvengadam R, Desiraju BK, Bhatnagar S, Salunke DM, Rashid F, Malakar D, Maiti TK and GARBH-Ini Study Group (2021) Dynamic Alteration in the Vaginal Secretory Proteome across the Early and Mid-Trimesters of Pregnancy. J Proteome Res 20:1190.
  8. Basak T, Dey AK, Banerjee R, Paul S, Maiti TK, and Ain R. Sequestration of eIF4A by angiomotin: A novel mechanism to restrict global protein synthesis in trophoblast cells (2021) Stem Cells 39:210.
  9. Hussain N, Chatterjee SK, Maiti TK, Goswami L, Das S, and Deb U, Bhattacharya SS. (2021) Metal induced non-metallothionein protein in earthworm: A new pathway for cadmium detoxification in chloragogenous tissue. J Hazard Mater 401:123357
  10. Kumari M, Hanpude P, and Maiti TK (2020) α-Synuclein Exhibits Differential Membrane Perturbation, Nucleation, and TLR2 Binding through Its Secondary Structure. (2020) ACS Chem Neurosci 11: 4203
  11. Dey AK, Kumar B, Singh AK, Ranjan P, Thiruvengadam R, Desiraju BK, Kshetrapal P, Wadhwa N, Bhatnagar S, Rashid F, Malakar D, Salunke DM, Maiti TK and GARBH-Ini Study Group (2020) Salivary proteome signatures in the early and middle stages of human pregnancy with term birth outcome. Scientific Reports 10: 8022
  12. Kumari R, Kumar R, Kumar S, Singh AK, Hanpude P, Jangir D, and Maiti TK. (2020) Amyloid aggregates of the deubiquitinase OTUB1 are neurotoxic, suggesting that they contribute to the development of Parkinson's disease. J Biol Chem 295:3466.
  13. Pant A, Bag S, Saha B, Verma J, Kumar P, Banerjee S, Kumar B, Kumar Y, Desigamani A, Maiti S, Maiti TK, Banerjee SK, Bhadra RK, Koley H, Dutta S, Nair GB, Ramamurthy T, and Das B. Molecular insights into the genome dynamics and interactions between core and acquired genomes of Vibrio cholerae. (2020) Proc Natl Acad Sci USA 117:23762.
  14. Zaman NR, Kumar B, Nasrin Z, Islam MR, Maiti TK, and Khan H. (2020) Proteome Analyses Reveal Macrophomina phaseolina's Survival Tools When Challenged by Burkholderia contaminans NZ. ACS Omega 5:1352.
  15. Kumar R, Kumar S, Hanpude P, Singh AK, Johari T, Majumder S, Maiti TK. (2019) Partially oxidized DJ-1 inhibits primary and secondary nucleation through adhesive surface and remodels mature α-synuclein fibrils to toxic conformations. Communications Biology | 2:395
  16. Puraswani M, Khandelwal P, Saini H, Saini S, Gurjar BS, Sinha A, Shende RP, Maiti TK, Singh AK, Kanga U, Ali U, Agarwal I, Anand K, Padmaraj Rajendran NP, Sinha R, Vasudevan A, Saxena A, Agarwal SK, Hari P, Sahu A, Rath S, Bagga A (2019) Clinical and immunological profile of anti-factor H antibody associated atypical hemolytic uremic syndrome: A nationwide database, Frontiers in Immunology | 10:1282
  17. Verma J, Bag S, Saha B, Kumar P, Ghosh TS, Dayal M, Dey P, Anbumani D, Kumar D, Rana P, Kumar B, Maiti TK, Sharma NC, Bhadra RK, Mutreja A, Nair GB, Ramamurthy T, Das B (2019) Genomic Plasticity associated with the antimicrobial resistance in Vibrio cholerae. Proc. Natl. Acad. Sci. USA | 116:6226.
  18. Das S, Kumar P, Verma A., Maiti TK, Mathew SJ (2019) Myosin heavy chain mutations that cause Freeman-Sheldon syndrome lead to muscle structural and functional defects in Drosophila. Developmental Biology | 449:90
  19. Joharia T, Maiti TK. (2018) Catalytic domain mutation in CYLD inactivates its enzyme function by structural perturbation and induces cell migration and proliferation Biochimica et Biophysica Acta | 1862:2081.
  20. 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 19:1129
  21. 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
  22. 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
  23. Hanpude P, Bhattacharya S, Singh AK, Maiti TK. (2017) Ubiquitin Recognition of BAP1: Understanding its Enzymatic Function. Biosci Rep 37
  24. 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
  25. 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
  26. 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
  27. 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
  28. Hanpude P, Bhattacharya S, Dey AK, Maiti TK (2015)  Deubiquitinating enzymes in cellular signaling and disease regulation. IUBMB Life 67:544.
  29. Maiti TK, Yamada K, Inoue K, Kandori H. (2012) L105K Mutant of Proteorhodopsin. Biochemistry 51:3198.
  30. 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.
  31. 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.
  32. 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.
  33. 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.
  34. 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.
  35. Ghosh KS, Maiti TK, Debnath J, Dasgupta S. (2007) Inhibition of Ribonuclease A by polyphenols present in green tea. Proteins 69:566.
  36. Chatterjee J, Maiti TK, Dasgupta S. (2006) Isolation and partial characterization of ribonuclease inhibitor from goat liver. Protein Pept Lett 13:779.
  37. 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.
  38. 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.
  39. 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.
  40. 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.
  41. 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.
  42. 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.
  43. Ghosh KS, Maiti TK, Dasgupta S. (2004) Green tea polyphenols as inhibitors of ribonuclease A. Biochem Biophys Res Commun 325:807.
  44. 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.
  45. 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
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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