CSIR - Centre for Cellular & Molecular Biology
Council of Scientific and Industrial Research
Ministry of Science & Technology, Govt. of India
Senior Scientist
Email: saikat@ccmb.res.in
Phone: +91 (0)40-2719 2572
We are interested in understanding the civil and mechanical engineering marvels within cells. Just like rebar and cables, which provide support to buildings and bridges, support structures of cells are made up of filamentous cytoskeletal elements like actin, microtubule and intermediate filaments. These dictate cellular morphology, generate forces for cell migration, and form intracellular tracks for movement of molecular motor proteins. These networks are highly regulated and are dynamic in nature. Different proteins interact with these filaments and regulate their polymerization, dissociation, or mediate connectivity between them. Deregulation or anomalies of the cytoskeletal network are associated with wide range of diseases like developmental disorders, neurodegeneration, delayed wound healing, and cancer metastasis.
Our lab's research focuses towards understanding how different cytoskeletal elements work in unison inside the cell, investigate the molecular basis of regulation of these networks, and how these participate in important cellular functions. We use cutting edge cryo-electron microscopy (cryo-EM), novel image processing methodologies along with biochemical and biophysical techniques to decode these cellular engineering feats.
Google Scholar page https://scholar.google.com/citations?hl=en&user=6-Tk-uUAAAAJ
Selected Publications
Shaaban, M., Chowdhury, S.#, Nolen, B.J.† Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state. Nature Structural & Molecular Biology. (2020); 27:1009-10016. DOI: https://doi.org/10.1038/s41594-020-0481-x . (#Corresponding author)
Rollins, M.F.*, Chowdhury, S.*, Carter, J., Golden, S.M., Miettinen, H.M., Santiago-Frangos, A., Faith, D., Lawrence, C.M., Lander, G.C., Wiedenheft, B. Structure reveals a mechanism of CRISPR-RNA guided nuclease recruitment and anti-CRISPR viral mimicry. Molecular Cell. (2019); 74(1):132-142. DOI: https://doi.org/10.1016/j.molcel.2019.02.001. (*Co-first author)
Chowdhury, S., Otomo, C., Leitner, A., Ohashi, K., Aebersold, R., Lander, G.C., Otomo, T. Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex. Proceedings of the National Academy of Sciences, USA. (2018); 115(42):E9792-E9801. DOI: https://doi.org/10.1073/pnas.1811874115.
Grotjahn DA*, Chowdhury S.*, Xu, Y., McKenney, R.J., Schroer, T.A., Lander, G.C. Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility. Nature Structural & Molecular Biology. (2018); 25(3):203-207. DOI: https://www.nature.com/articles/s41594-018-0027-7. (*Co-first author)
Chowdhury, S., Carter, J., Rollins, M.F., Golden, S.M., Jackson, R.N., Hoffmann, C., Nosaka, L., Bondy-Denomy, J., Maxwell, K.L., Davidson, A.R., Fischer, E.R., Lander, G.C., Wiedenheft, B. Structure reveals mechanisms of viral suppressors that Intercept a CRISPR RNA-guided surveillance complex. Cell. (2017); 169(1):47-57.e11. DOI: https://doi.org/10.1016/j.cell.2017.03.012.
Chowdhury, S., Ketcham, S.A., Schroer, T.A., Lander, G.C. Structural organization of the dynein-dynactin complex bound to microtubules. Nature Structural & Molecular Biology. (2015); 22(4):345-7. DOI: https://doi.org/10.1016/j.cell.2017.03.012.
Education & Experience
P.G: | B.Tech-Bioinformatics ; Vellore Institute of Technology, Vellore, Tamil Nadu, India ; 2002-2006 |
Ph.D: | The Pennsylvania State University, University Park, Pennsylvania, USA ; (2006-2012) ; |
Post.Doc: | Scripps Research, La Jolla, California, USA ; (2012-2018) ; |
Experience: | Assistant Professor: (2018-2021) Dept. of Biochemistry & Cell Biology, SUNY Stony Brook University, Stony Brook, New York, USA
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Title | Journal | Year |
---|---|---|
Arf GTPase activates the WAVE regulatory complex through a distinct binding site | Science Advances | 2022 |
Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase | Nature Communications | 2022 |
Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy. | Proceedings of the National Academy of Sciences, USA | 2022 |
Structural basis of piRNA targeting. | Nature | 2021 |
Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state. | Nature Structural & Molecular Biology (https://doi.org/10.1038/s41594-020-0481-x) | 2020 |
A guided approach for subtomogram averaging of challenging macromolecular assemblies. | Journal of Structural Biology:X (https://doi.org/10.1016/j.yjsbx.2020.100041) | 2020 |
Structure reveals a mechanism of CRISPR-RNA guided nuclease recruitment and anti-CRISPR viral mimicry. | Molecular Cell (https://doi.org/10.1016/j.molcel.2019.02.001) | 2019 |
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. | Nature Communications (https://doi.org/10.1038/s41467-017-02474-4) | 2018 |
Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility. | Nature Structural & Molecular Biology (https://doi.org/10.1038/s41594-018-0027-7) | 2018 |
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex. | Proceedings of the National Academy of Sciences, USA (https://doi.org/10.1073/pnas.1811874115) | 2018 |
The rod-shaped ATG2A-WIPI4 complex tethers membranes in vitro. | Contact (https://doi.org/10.1177%2F2515256418819936) | 2018 |
Structure reveals mechanisms of viral suppressors that Intercept a CRISPR RNA-guided surveillance complex. | Cell (https://doi.org/10.1016/j.cell.2017.03.012) | 2017 |
Cas1 and the Csy complex are opposing regulators of Cas2/3 nuclease activity. | Proceedings of the National Academy of Sciences, USA (https://doi.org/10.1073/pnas.1616395114) | 2017 |
The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer. | The EMBO Journal (https://doi.org/10.15252/embj.201695616) | 2017 |
The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. | Journal of Molecular Biology (https://doi.org/10.1016/j.jmb.2015.01.019) | 2015 |
Structural organization of the dynein-dynactin complex bound to microtubules. | Nature Structural & Molecular Biology (https://doi.org/10.1038/nsmb.2996) | 2015 |
Breaking symmetry in multimeric ATPase motors. | Cell Cycle (https://doi.org/10.4161/cc.28957) | 2014 |
Nucleotide-induced asymmetry within ATPase activator ring drives Sigma54-RNAP interaction and ATP hydrolysis. | Genes & Development (https://doi.org/10.1101/gad.229385.113) | 2013 |
Opening and closing of the bacterial RNA polymerase clamp. | Science (https://doi.org/10.1126/science.1218716) | 2012 |
Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. | Structure (https://doi.org/10.1016/j.str.2010.08.018) | 2010 |
ADPase activity of recombinantly expressed thermotolerant ATPases may be caused by copurification of adenylate kinase of Escherichia coli. | The FEBS Journal (https://doi.org/10.1111/j.1742-4658.2008.06825.x) | 2009 |
Regulation and action of the bacterial enhancer-binding protein AAA+ domains. | Biochemical Society Transactions (https://doi.org/10.1042/BST0360089) | 2008 |
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