Honors & Awards

  • HHMI International Student Research Fellowship, HHMI (2012-2015)
  • Dissertation Completion Fellowship, University of North Carolina at Chapel Hill (2015-2016)

Professional Education

  • Bachelor of Technology, Indian Institute of Technology, Kharagpur, Biotechnology (2010)
  • Master of Technology, Indian Institute of Technology, Kharagpur (2010)
  • Doctor of Philosophy, University of North Carolina, Chapel Hill (2016)

Stanford Advisors


All Publications

  • Crescerin uses a TOG domain array to regulate microtubules in the primary cilium MOLECULAR BIOLOGY OF THE CELL Das, A., Dickinson, D. J., Wood, C. C., Goldstein, B., Slep, K. C. 2015; 26 (23): 4248-4264


    Eukaryotic cilia are cell-surface projections critical for sensing the extracellular environment. Defects in cilia structure and function result in a broad range of developmental and sensory disorders. However, mechanisms that regulate the microtubule (MT)-based scaffold forming the cilia core are poorly understood. TOG domain array-containing proteins ch-TOG and CLASP are key regulators of cytoplasmic MTs. Whether TOG array proteins also regulate ciliary MTs is unknown. Here we identify the conserved Crescerin protein family as a cilia-specific, TOG array-containing MT regulator. We present the crystal structure of mammalian Crescerin1 TOG2, revealing a canonical TOG fold with conserved tubulin-binding determinants. Crescerin1's TOG domains possess inherent MT-binding activity and promote MT polymerization in vitro. Using Cas9-triggered homologous recombination in Caenorhabditis elegans, we demonstrate that the worm Crescerin family member CHE-12 requires TOG domain-dependent tubulin-binding activity for sensory cilia development. Thus, Crescerin expands the TOG domain array-based MT regulatory paradigm beyond ch-TOG and CLASP, representing a distinct regulator of cilia structure.

    View details for DOI 10.1091/mbc.E15-08-0603

    View details for Web of Science ID 000366325800007

    View details for PubMedID 26378256