Nuclear pore exclusively mediate all the transport that take place between nucleus and cytoplasm. These pores are made up of protein called Nups and these Nups play critical regulatory roles in nucelo-cytoplasmic transport. 

We are exploring the importance of Nups during development utilizing Drosophila melanogaster as model organism. We are investigating functions of the dELYS and the Nup107-160 complex in organismal growth and development through biochemical and genetic interventions. dELYS play critical roles in Drosophila development through regulation of Dorsal pathway. In particular, we are dissecting out dELYS function in hematopoeitic development and Nup107 complex role in neuronal development and signaling.

Nups are known to be dysregulated in cancer. Chromosomal translocation mediated roles of Nups in cancer was known for long. Over-expression of Nups is being appreciated lately, for their involvement in cancer. Expression levels of Nups like Nup88 and Nup107 can be correlated with cancer progression and metastasis. Nup over-expression is suggested to cause an imbalance of transport and abnormalities in cell division. 

Biochemical and cell biological analysis of important regulators of Nup88 and Nup107 is an important aspects of this study. How these nuclear pore proteins help regulate cell division by mediating nucleo-cytoplasmic transport is a piece of puzzle that we are trying to put together.

Post translation modification by SUMO is known to play important role in regulating localization and function of many proteins including transcription factors, signaling molecules etc. Extensive work on SUMO suggests that the C-terminal region harbors interaction sites for substrate and enzymes of the pathway.

          Characterization of SUMO modification machinery in the causative agent for malaria, Plasmodium falciparum, has got us interested in under-standing this pathway in further detail. We are keenly pursuing the idea of identifying SUMO substrates critical for Plasmodium survival. We are also exploring the importance of sumo machinery in infection and malaria pathogenesis. 

SUMOylation of cytolinker protein PPL by SUMO1 is enhanced under cytoskeletal rearrangement. The non-SUMOylatable PPL (PPL-K1646R) affects the stability and organization of Keratin intermediate filament (IF). Periplakin SUMOylation mutant induce precocious collapse of keratin IF when stressed. PPL is known desmosomal protein and it can affect the integrity of cells in epithelium.

We are developing an understanding of how SUMOylation of PPL affects intermediate filament dynamics. How the interactions of PPL would affect the Keratin filament assembly? 

Several methods have described in greater details for the labeling of proteins for academic and therapeutics purposes. However, most of them are not precise in term of labeling proteins uniquely. Proteins modified using the Linchpin Directed modification (LDM) and other related chemical toolboxes available with Dr. Vishal Rai's group in the Chemistry Department, IISER Bhopal, we are involved in the precise in vitro and in cellula labeling and characterization of proteins.