RT Journal Article
SR Electronic
T1 Microtubule glycylation promotes basal body attachment to the cell cortex
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 620476
DO 10.1101/620476
A1 Anthony D. Junker
A1 Adam W. J. Soh
A1 Eileen T. O’Toole
A1 Janet B. Meehl
A1 Mayukh Guha
A1 Mark Winey
A1 Jerry E. Honts
A1 Jacek Gaertig
A1 Chad G. Pearson
YR 2019
UL http://biorxiv.org/content/early/2019/04/26/620476.abstract
AB Motile cilia generate directed hydrodynamic flow that is important for the motility of cells and extracellular fluids. To optimize directed hydrodynamic flow, motile cilia are organized and oriented into a polarized array. Basal bodies (BB) nucleate and position motile cilia at the cell cortex. Cytoplasmic BB-associated microtubules are conserved structures that extend from BBs. Using the ciliate, Tetrahymena thermophila, combined with EM-tomography and light microscopy, we show that BB-appendage microtubules assemble coincident with new BB assembly and are attached to the cell cortex. These BB-appendage microtubules are specifically marked with post translational modifications of tubulin, including glycylation. Mutations that prevent glycylation shorten BB-appendage microtubules and disrupt BB positioning and cortical attachment. Consistent with the attachment of BB-appendage microtubules to the cell cortex for BB positioning, mutations that disrupt the cellular cortical cytoskeleton similarly disrupt the cortical attachment and positioning of BBs. In summary, BB-appendage microtubules promote the organization of ciliary arrays through attachment to the cell cortex.SUMMARY STATEMENT Basal bodies position motile cilia at the cell cortex. This study finds tubulin glycylation to promote BB-associated microtubule elongation and structural attachment of basal bodies to the cell’s cortical cytoskeleton.BBbasal bodiesSFstriated fibertMTtransverse microtubulepcMTpost-ciliary microtubuleMTmicrotubulePTMpost-translational modification