CCMB

CSIR - Centre for Cellular & Molecular Biology

The Innovation Engine of India

Saikat Chowdhury

Saikat Chowdhury

Saikat Chowdhury

Scientist-E
Structural biology of macromolecular machinery and cryo-electron microscopy
+91 (0)40-2719 2572
saikat@ccmb.res.in

Research Interests
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 labs 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:

Scripps Research, La Jolla, California, USA ; (2012-2018) ;

Post.Doc:

Assistant Professor: (2018-2021) Dept. of Biochemistry & Cell Biology, SUNY Stony Brook University, Stony Brook, New York, USA
Adjunct Assistant Professor: (2021-2024) Dept. of Biochemistry & Cell Biology, SUNY Stony Brook University, Stony Brook, New York, USA

Experience:

Assistant Professor: (2018-2021) Dept. of Biochemistry & Cell Biology, SUNY Stony Brook University, Stony Brook, New York, USA
Adjunct Assistant Professor: (2021-2024) Dept. of Biochemistry & Cell Biology, SUNY Stony Brook University, Stony Brook, New York, USA

Team Members

team-members-pic
Saikat Chowdhury
Saikat Chowdhury

Scientist-E

Scientist-E

Ravikumar Reddi
Ravikumar Reddi

Scientist-C

Scientist-C

A Harikrishna
A Harikrishna

Sr. Technical Officer(3)

Sr. Technical Officer(3)

Sandeep Shrivastava
Sandeep Shrivastava

Sr. Technical Officer(2)

Sr. Technical Officer(2)

Justus Francis
Justus Francis

Junior Research Fellow

Junior Research Fellow

Pathri Achyutha Krishna
Pathri Achyutha Krishna

Junior Research Fellow

Junior Research Fellow

Palash Kumar Seal
Palash Kumar Seal

Junior Research Fellow

Junior Research Fellow

Amarttya Bagchi
Amarttya Bagchi

Junior Research Fellow

Junior Research Fellow

Rishav Mitra
Rishav Mitra

Project Associate-I

Project Associate-I

Publications

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/10.11772515256418819936)
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
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
Regulation and action of the bacterial enhancer-binding protein AAA+ domains.
Biochemical Society Transactions (https://doi.org/10.1042/BST0360089)
2008
Regulation and action of the bacterial enhancer-binding protein AAA+ domains.
Biochemical Society Transactions (https://doi.org/10.1042/BST0360089)
2008
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
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

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