Shehani Kahawatte

ORCID: 0009-0003-6997-0507
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About
Contact & Profiles
Research Areas
  • Microtubule and mitosis dynamics
  • Hereditary Neurological Disorders
  • Neurological diseases and metabolism
  • Machine Learning in Bioinformatics
  • Neurogenetic and Muscular Disorders Research
  • Cellular transport and secretion
  • Ubiquitin and proteasome pathways
  • RNA and protein synthesis mechanisms
  • Bacteriophages and microbial interactions
  • Glycosylation and Glycoproteins Research
  • Microbial Metabolic Engineering and Bioproduction
  • Cellular Mechanics and Interactions
  • Bioinformatics and Genomic Networks
  • RNA Research and Splicing
  • Receptor Mechanisms and Signaling
  • Peptidase Inhibition and Analysis
  • Computational Drug Discovery Methods

University of Cincinnati
2023-2025

Spastin is a microtubule-severing AAA+ ATPase that highly expressed in neuronal cells and plays crucial role axonal growth, branching, regeneration. This machine oligomerizes into hexamers the presence of ATP microtubule carboxy-terminal tails (CTTs). Conformational changes spastin hexamers, powered by hydrolysis, apply forces to microtubule, ultimately leading severing filament. Mutations disrupt normal function spastin, impairing its ability sever microtubules effectively abnormal dynamics...

10.1021/acs.biochem.4c00693 article EN Biochemistry 2025-02-26

The nanomachine from the ATPases associated with various cellular activities superfamily, called spastin, severs microtubules during processes. To characterize functionally important allostery in we employed methods evolutionary information, to graph-based networks, machine learning applied atomistic molecular dynamics simulations of spastin its monomeric and functional hexameric forms, presence or absence ligands. Feature selection, using approaches, for transitions between states...

10.1063/5.0139273 article EN The Journal of Chemical Physics 2023-03-07

In cells, microtubule location, length, and dynamics are regulated by a host of microtubule-associated proteins enzymes that read where to bind act based on the “tubulin code,” which is predominantly encoded in tubulin carboxy-terminal tail (CTT). Katanin highly conserved AAA ATPase enzyme binds CTTs remove dimers sever microtubules. We have previously demonstrated short CTT peptides able inhibit katanin severing. Here, we examine effects sequences this inhibition activity. Specifically,...

10.3390/biom13040620 article EN cc-by Biomolecules 2023-03-30

In celIs, microtubule location, length, and dynamics are regulated by a host of microtubule-associated proteins enzymes that read where to bind act based on the “tubulin code,” which is predominantly encoded in tubulin carboxy-terminal tail (CTT). Katanin highly conserved AAA ATPase enzyme binds CTTs remove dimers sever microtubules. We have previously demonstrated short CTT peptides able inhibit katanin severing. Here, we examine effects sequences this inhibition...

10.20944/preprints202301.0344.v1 preprint EN 2023-01-19

Abstract Spastin is a microtubule-severing AAA+ ATPase that highly expressed in neu-ronal cells and plays crucial role axonal growth, branching, regeneration. This machine oligomerizes into hexamers the presence of ATP microtubule carboxy-terminal tails (CTTs). Conformational changes spastin hexamers, pow-ered by hydrolysis, apply forces on microtubule, ultimately leading to severing filament. Mutations disrupt normal function spastin, impair-ing its ability sever microtubules effectively...

10.1101/2024.10.17.618886 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-10-18
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