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- W2079665723 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." @default.
- W2079665723 created "2016-06-24" @default.
- W2079665723 creator A5026761544 @default.
- W2079665723 creator A5091261902 @default.
- W2079665723 date "2010-10-01" @default.
- W2079665723 modified "2023-10-05" @default.
- W2079665723 title "Patronin Regulates the Microtubule Network by Protecting Microtubule Minus Ends" @default.
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- W2079665723 doi "https://doi.org/10.1016/j.cell.2010.09.022" @default.
- W2079665723 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3008421" @default.
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