Faculty Opinions recommendation of Patronin regulates the microtubule network by protecting microtubule minus ends.
Year: 2010
Type: peer-review
Abstract: Tubulin assembles into microtubule polymers that have distinct plus and minus ends. Most microtubule plus ends in living cells are dynamic; the transitions between growth and shrinkage are regulated by assembly-promoting and destabilizing proteins. In contrast, minus ends are generally not dynamic, suggesting their stabilization by some unknown protein. Here, we have identified Patronin (also known as ssp4) as a protein that stabilizes microtubule minus ends in Drosophila S2 cells. In the absence of Patronin, minus ends lose subunits through the actions of the Kinesin-13 microtubule depolymerase, leading to a sparse interphase microtubule array and short, disorganized mitotic spindles. In vitro, the selective binding of purified Patronin to microtubule minus ends is sufficient to protect them against Kinesin-13-induced depolymerization. We propose that Patronin caps and stabilizes microtubule minus ends, an activity that serves a critical role in the organization of the microtubule cytoskeleton.Copyright © 2010 Elsevier Inc. All rights reserved. PMID: 20946984 Funding information This work was supported by: NIGMS NIH HHS, United States Grant ID: R37 GM038499-22 NIGMS NIH HHS, United States Grant ID: R37 GM038499 Howard Hughes Medical Institute, United States
Authors: Gaudenz Danuser, Jessica Tytell
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W4205535354