| Snail destabilizes cell surface Crumbs3a. | |
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MedLine Citation:
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PMID: 22554228 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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During epithelial to mesenchymal transition (EMT), cells modulate expression of proteins resulting in loss of apical-basal polarity. Effectors of this EMT switch target the polarity protein Crumbs3a, a small transmembrane protein that is essential for generation of the apical membrane and tight junctions of mammalian epithelial cells. We previously showed that the Crumbs3 gene is a direct target of transcriptional regulation by Snail, a potent inducer of EMT. However, Snail has also been shown to have multiple non-transcriptional roles, including regulation of cell adhesion, proliferation and survival. Using SNAP-tag labeling, we determined that cell surface Crumbs3a has a half-life of approximately 3 h and that this cell surface half-life is significantly reduced when EMT is induced by Snail. We further observe that Snail induces differential glycosylation of Crumbs3a, including sialylation, suggesting a mechanism by which Crumbs3a may be destabilized. These results indicate that Crumbs3a is a post-translational target of Snail, in addition to being a transcriptional target. We conclude that Snail's ability to post-translationally modify and destabilize Crumbs3a augments the depolarizing process of EMT. |
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Authors:
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Jennifer L Harder; Eileen L Whiteman; Jay N Pieczynski; Chia-Jen Liu; Ben Margolis |
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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: 2012-05-28 |
Journal Detail:
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Title: Traffic (Copenhagen, Denmark) Volume: 13 ISSN: 1600-0854 ISO Abbreviation: Traffic Publication Date: 2012 Aug |
Date Detail:
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Created Date: 2012-07-13 Completed Date: 2012-11-19 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 100939340 Medline TA: Traffic Country: Denmark |
Other Details:
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Languages: eng Pagination: 1170-85 Citation Subset: IM |
Copyright Information:
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© 2012 John Wiley & Sons A/S. |
Affiliation:
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Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Line Cell Membrane / metabolism Dogs Epithelial Cells / metabolism Epithelial-Mesenchymal Transition Glycosylation Humans Membrane Glycoproteins / metabolism* Protein Processing, Post-Translational Protein Stability Tight Junctions / metabolism Transcription Factors / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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DK020572/DK/NIDDK NIH HHS; F32GM079906/GM/NIGMS NIH HHS; R01 DK069605/DK/NIDDK NIH HHS; R01DK058208/DK/NIDDK NIH HHS; R01DK069605/DK/NIDDK NIH HHS; T32DK007378/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/CRB3 protein, human; 0/Membrane Glycoproteins; 0/Transcription Factors; 0/snail family transcription factors |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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