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. 1999 Jul 12;146(1):13–28. doi: 10.1083/jcb.146.1.13

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Distribution of 3F3/2 phosphoepitopes in bub1 mutant neuroblasts. DNA is in blue, and 3F3/2 phosphoepitopes are in green. In all panels, the two strongest sites of 3F3/2 staining are the centrosomes. 3F3/2 distribution in prophase (A) and metaphase (B) neuroblasts from bub1 mutants. 3F3/2 epitopes at the centrosomes and kinetochores are strongly recognized, demonstrating that the Bub1 kinase is not a significant source of 3F3/2 phosphorylation activity in vivo. (C) 3F3/2 epitopes are completely dephosphorylated during anaphase in wild-type neuroblasts (see Bousbaa et al. 1997 for a detailed description of 3F3/2 distribution in wild-type Drosophila neuroblasts). (D) 3F3/2 distribution in an anaphase figure from a bub1 mutant neuroblast. 3F3/2 epitopes continue to remain phosphorylated in bub1 anaphases, though at reduced levels relative to those seen during prophase/prometaphase. Thus, total dephosphorylation of 3F3/2 phosphoepitopes cannot be a prerequisite for entry into anaphase. Bar, 5 μm.