How tubulin and kinesin gene families specialize microtubule networks

The National Institute of General Medical Sciences awarded The Regents Of The University Of Colorado, doing business as University Of Colorado-Denver, $296,757 under the Biomedical Research and Research Training program (CFDA 93.859) on July 10, 2026. The project investigates how tubulin and kinesin gene families specialize microtubule networks, addressing two critical knowledge gaps: the mechanistic role of tubulin isotypes in generating programs of tubulin post-translational modifications, and expanding the inventory of proteins that read the tubulin code and understanding how reading impacts function. The award obligates $296,757 and runs through April 30, 2030, with place of performance in Aurora, Colorado.

Abstract

Our understanding of the inventory of genetically encoded and post-translationally modified forms of cytoskeletal proteins has grown immensely over the last 20 years. IT is now clear that microtubule networks are not uniform tracks that are traversed by a common set of motor proteins. Instead, the tubulin subunits of microtubules can sample a variety of structural and biochemical states, creating the potential for molecularly distinct microtubule tracks that are specific to different cell types, or even specific to different compartments of the same cell. Similarly, the large family of kinesin genes and even larger family of kinesin proteoforms creates potential for distinct modes of transport and force generation along microtubules. Understanding of how cells use these inventories to create a range of specific biological outcomes now represents a critical knowledge GAP in cytoskeletal biology. This project will address two major knowledge gaps that are critical for the tubulin code model, and also broadly important for the microtubule field: 1) the mechanistic role(s) of tubulin isotypes in generating programs of tubulin ptms, and 2) expanding the inventory of maps that read the tubulin code and understanding how reading impacts function.