IISER Mohali, Knowledge city, Sector 81, SAS Nagar, Manauli PO 140306

Dr. Shravan Kumar Mishra
Assistant Professor, Biological Sciences

Contact ABII-3F3 (Office) & ABII-4L2 (Lab)  
Email skmishra(AT)iisermohali.ac.in
Fax +91 172 2240266
ORCID ID https://orcid.org/0000-0003-3899-0495
Personal Page          


Research Area
Molecular Cell Biology
Research Topics
Ubiquitin-Like Modifiers and Control of Pre-mRNA Splicing


Research Focus

We study function and regulation of proteins related to ubiquitin in cellular processes of pre-messenger RNA splicing and signaling. For these studies we perform experiments in molecular cell biology, genetics, and biochemistry in the budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe. We use mammalian cell cultures and multi-cellular organisms through collaborations to highlight functional conservations of the findings made in these organisms and their potential applications to humans.

Ubiquitin and ubiquitin-like modifiers, for example, Hub1, SUMO, NEDD8, Sde2 etc., are a group of small proteins harboring ubiquitin fold, and function as central regulators for a large number of processes in the cell. The covalent attachment of ubiquitin to target proteins, termed ubiquitination, requires a set of dedicated enzymes. The process of ubiquitination is key for determining fate of target proteins through their degradation in the proteasome. The process also diversifies functions of its targets by modulating their properties in non-proteolytic ways. Other ubiquitin-like modifiers also attach to target proteins as modules or tags, both covalently and non-covalently, and play regulatory roles a similar large number of processes. These modifiers often operate as molecular switch in processes such DNA repair, signal transduction, protein sorting etc.

The ubiquitin-like protein Hub1 is conserved from budding yeast to humans. It binds to splicing factors non-covalently, and functions in pre-mRNA splicing in a unique way, for efficient splicing of a subset of introns and to promote alternative splicing. The ubiquitin-fold harboring Sde2 is conserved in intron-rich eukaryotes from fission yeast to humans. The protein gets incorporated in the splicing machinery, spliceosome, for intron-specific pre-mRNA splicing after cleavage of its ubiquitin fold by specific deubiquitinating enzymes. Defects in heterochromatin silencing and genome stability are known to be hallmarks of many diseases including cancer. Our recent discoveries suggest that the process of intron-specific pre-mRNA splicing becomes critical for heterochromatin silencing and genome stability.

Selected Publications


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