| Gradients of a ubiquitin E3 ligase inhibitor and a caspase inhibitor determine differentiation or death in spermatids. | |
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MedLine Citation:
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PMID: 20643358 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Caspases are executioners of apoptosis but also participate in a variety of vital cellular processes. Here, we identified Soti, an inhibitor of the Cullin-3-based E3 ubiquitin ligase complex required for caspase activation during Drosophila spermatid terminal differentiation (individualization). We further provide evidence that the giant inhibitor of apoptosis-like protein dBruce is a target for the Cullin-3-based complex, and that Soti competes with dBruce for binding to Klhl10, the E3 substrate recruitment subunit. We then demonstrate that Soti is expressed in a subcellular gradient within spermatids and in turn promotes proper formation of a similar dBruce gradient. Consequently, caspase activation occurs in an inverse graded fashion, such that the regions of the developing spermatid that are the last to individualize experience the lowest levels of activated caspases. These findings elucidate how the spatial regulation of caspase activation can permit caspase-dependent differentiation while preventing full-blown apoptosis. |
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Authors:
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Yosef Kaplan; Liron Gibbs-Bar; Yossi Kalifa; Yael Feinstein-Rotkopf; Eli Arama |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Developmental cell Volume: 19 ISSN: 1878-1551 ISO Abbreviation: Dev. Cell Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-07-20 Completed Date: 2010-08-30 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101120028 Medline TA: Dev Cell Country: United States |
Other Details:
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Languages: eng Pagination: 160-73 Citation Subset: IM |
Copyright Information:
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(c) 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis / physiology Caspases / antagonists & inhibitors* Cell Differentiation / physiology Cullin Proteins / genetics, metabolism Drosophila Proteins / genetics, metabolism Drosophila melanogaster / cytology, genetics, metabolism Enzyme Inhibitors / metabolism Genes, Insect Male Models, Biological Mutation Saccharomyces cerevisiae / metabolism Spermatids / cytology*, metabolism* Spermatogenesis / genetics, physiology Ubiquitin-Protein Ligases / antagonists & inhibitors* |
| Chemical | |
Reg. No./Substance:
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0/Bruce protein, Drosophila; 0/Cullin Proteins; 0/Drosophila Proteins; 0/Enzyme Inhibitors; 0/gft protein, Drosophila; EC 3.4.22.-/Caspases; EC 6.3.2.19/Ubiquitin-Protein Ligases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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