| TEX14 interacts with CEP55 to block cell abscission. | |
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MedLine Citation:
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PMID: 20176808 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In somatic cells, abscission, the physical separation of daughter cells at the completion of cytokinesis, requires CEP55, ALIX, and TSG101. In contrast, cytokinesis is arrested prior to abscission in differentiating male germ cells that are interconnected by TEX14-positive intercellular bridges. We have previously shown that targeted deletion of TEX14 disrupts intercellular bridges in all germ cells and causes male sterility. Although these findings demonstrate that intercellular bridges are essential for spermatogenesis, it remains to be shown how TEX14 and other proteins come together to prevent abscission and form stable intercellular bridges. Using a biochemical enrichment of male germ cell intercellular bridges, we identified additional bridge proteins, including CEP55. Although CEP55 is highly expressed in testes at the RNA level, there is no report of the presence of CEP55 in germ cells. We show here that CEP55 becomes a stable component of the intercellular bridge and that an evolutionarily conserved GPPX3Y motif of TEX14 binds strongly to CEP55 to block similar GPPX3Y motifs of ALIX and TSG101 from interacting and localizing to the midbody. Thus, TEX14 prevents the completion of cytokinesis by altering the destiny of CEP55 from a nidus for abscission to an integral component of the intercellular bridge. |
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Authors:
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Tokuko Iwamori; Naoki Iwamori; Lang Ma; Mark A Edson; Michael P Greenbaum; Martin M Matzuk |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2010-02-22 |
Journal Detail:
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Title: Molecular and cellular biology Volume: 30 ISSN: 1098-5549 ISO Abbreviation: Mol. Cell. Biol. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-04-08 Completed Date: 2010-04-22 Revised Date: 2010-11-02 |
Medline Journal Info:
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Nlm Unique ID: 8109087 Medline TA: Mol Cell Biol Country: United States |
Other Details:
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Languages: eng Pagination: 2280-92 Citation Subset: IM |
Affiliation:
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Department of Pathology, Baylor College of Medicine, One Baylor Plaza, S217, Houston, TX 77030, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Animals Calcium-Binding Proteins / metabolism Cell Line Conserved Sequence Cytokinesis* DNA-Binding Proteins / metabolism Endosomal Sorting Complexes Required for Transport / metabolism Female Humans Intercellular Junctions / metabolism Male Mice Models, Biological Molecular Sequence Data Mutant Proteins / chemistry, metabolism Nuclear Proteins / chemistry, metabolism* Ovary / cytology, metabolism Protein Binding Structure-Activity Relationship Testis / cytology, metabolism Transcription Factors / chemistry, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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R01HD057880/HD/NICHD NIH HHS; T32GM07330/GM/NIGMS NIH HHS; T32HD007165/HD/NICHD NIH HHS; U01HD060496/HD/NICHD NIH HHS; U54HD07495/HD/NICHD NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Calcium-Binding Proteins; 0/DNA-Binding Proteins; 0/Endosomal Sorting Complexes Required for Transport; 0/Mutant Proteins; 0/Nuclear Proteins; 0/Pdcd6ip protein, mouse; 0/TEX14 protein, human; 0/TEX14 protein, mouse; 0/Transcription Factors; 0/Tsg101 protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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