The alpha tubulin acetyltransferase atat-2 genetically interacts with klp-4 in C. elegans
Claire E Reist1, Michael D Webb2, Cortlen M Mathews2
1Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill.
Abstract:
Microtubules dynamics are in part regulated by post-translational modification, including acetylation. Little is known about the relationship between microtubule acetylation status and how this affects kinesin function, especially in vivo . Using a series of aldicarb sensitivity assays in C. elegans where we combined pharmacological manipulation of microtubule dynamics with genetic approaches, we demonstrate a specific genetic interaction between the alpha tubulin acetyltransferase atat-2 and the kinesin motor klp-4 . Our work highlights interactions between kinesin activity and the tubulin code in vivo and lays the foundation of future work on these two parallel, yet related processes in cells.
Related Concept Videos
Tail-anchoring of Proteins in the ER Membrane
Assembly of Complex Microtubule Structures
Microtubule Instability
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Microtubule Associated Proteins (MAPs)
Microtubule Formation


