Document Detail


TEX14 interacts with CEP55 to block cell abscission.
MedLine Citation:
PMID:  20176808     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Tokuko Iwamori; Naoki Iwamori; Lang Ma; Mark A Edson; Michael P Greenbaum; Martin M Matzuk
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-02-22
Journal Detail:
Title:  Molecular and cellular biology     Volume:  30     ISSN:  1098-5549     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-08     Completed Date:  2010-04-22     Revised Date:  2013-05-30    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2280-92     Citation Subset:  IM    
Affiliation:
Department of Pathology, Baylor College of Medicine, One Baylor Plaza, S217, Houston, TX 77030, USA.
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MeSH Terms
Descriptor/Qualifier:
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:
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:
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
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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