Projects

We are pursuing biochemical reconstitution and atomic resolution 3D structure determination of human Nup93 subcomplex, also known as inner ring complex and Nup62 sub-complex (known as central transport channel, CTC). We deciphered precise interaction regions of mammalian Nup93 that can be biochemically assembled with ordered region of Nup62•Nup54•Nup58 complex and showed EM structure using negatively stained method. We also demonstrated how the dynamic nature of the CTC complex is conserved across the species yet maintaining the species specific features.
See Biochemistry 2017, Protein Science 2019, Protein Science 2020

We also successfully reconstituted mammalian Nup88•Nup62•Nup214 complex and revealed the scaffold/hub role of Nup62 coiled-coil mediated heterotrimer formation with other Nups and such heterotrimers can be recognized by Nup93 based on 3D shape (biorxiv 2022)

We use cryo-EM Single particle analysis based methodologies to determine atomic resolution structure of human Nups, such as Nup155 (Biorxiv 2021) that revealed a biochemical consequences of a genetic mutation (R391H) to cause atria fibrilliation.

We are pursuing the physical interactions of human Nucleoporins with several viral factors to elucidate the underlying role of the NPC in viral infections such as HIV-1. (Cells 2019) 

Using the combination of biochemical methods and machine learning computational tools we are actively pursuing development of new methods to decipher interacting network of multiprotein complexes. Our efforts in this area led us to come up with a tool (CoRNeA) that can predict interacting regions between two partners solely based on their primary sequences. Such method is extremely beneficial in biochemical reconstitution of the multimeric proteins (Biomolecules 2020).

Nucleoporins forms condensates inside the cell which is essential for nucleocytoplasmic transport. We are exploring how different Nups are involved in establishing permeability barrier by using biophysical and biochemical techniques.