Bio

I am a postdoctoral researcher at Stanford University investigating how cytoskeletal regulators drive developmental processes and cellular pathways. My research focuses on the dynamic organization of the actin cytoskeleton and its roles in cell mechanics, asymmetric cell division, and embryonic development. I am particularly fascinated by how dynamic actin networks shape life at both the cellular and organismal levels. By integrating cell and developmental biology with quantitative imaging, molecular biology, and biophysical approaches, I aim to uncover the mechanisms that govern cellular behavior during development and inspire future advances in developmental biology and regenerative medicine.

Institute Affiliations

Stanford Advisors

Contact

  • Academic
    shubham7@stanford.edu
    University - Scholar Department: Biology Position: Postdoctoral Scholar

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All Publications

  • PIST couples actin cytoskeleton dynamics through a WH2-like actin-binding domain BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Dutta, P., Das, S., Bandyopadhyay, P., Das, S., Mazumder, M., Gourinath, S., Maiti, S. 2026; 837: 154604

    Abstract

    Purkinje cell synapses in the cerebellar cortex require tight coordination between receptor trafficking and cytoskeletal remodeling to sustain synaptogenesis, structural plasticity, and motor learning. The glutamate δ2 receptor (GluRδ2), a hallmark component of parallel fiber-Purkinje cell synapses, depends on intracellular scaffolding proteins for proper localization and signaling. PIST (GOPC), a neuronal PDZ domain-containing protein originally identified as a selective GluRδ2-interacting partner, has emerged as an important regulator of receptor trafficking and synaptic organization. Here, we reveal a previously unrecognized biochemical function of PIST as an actin-binding protein. Biochemical and cellular analyses show that PIST directly associates with filamentous actin in a concentration-dependent manner, suppresses actin polymerization in vitro, and co-localizes with actin in neuronal cells. Mechanistically, this interaction is mediated by a WH2-like motif within PIST. PIST may function as a molecular link between the actin cytoskeleton and the protein trafficking machinery, suggesting a potential new mechanism underlying the coordinated regulation of receptor transport and synaptic structural plasticity in neurons.

    View details for DOI 10.1016/j.bbrc.2026.154604

    View details for Web of Science ID 001884298900001

    View details for PubMedID 42767008

https://orcid.org/0000-0001-6379-9313