| Notch activation is regulated by an interaction between hCLP46 and chaperone protein calnexin. | |
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MedLine Citation:
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PMID: 22473674 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Human CAP10-like protein 46 kDa (hCLP46), as a protein O-glucosyltransferase in mammalian cell lines, modifies the epidermal growth factor-like repeat of Notch receptor and regulates Notch signal pathway, which plays a significant role in carcinogenesis of mammalian. O-glucosylation, modified by rumi in drosophila and poglut in mouse to Notch and other receptors with epidermal growth factor repeat, has been reported. In this article, we want to further study the regulation of interaction between hCLP46 and other associate chaperones to Notch signaling. The investigation shows that endoplasmic reticulum lectin calnexin as a chaperone protein interacts with hCLP46 in HEK293Trex cell lines by co-immunoprecipitation. Calnexin usually associates selectively with newly synthesized glycoprotein, promoting their proper folding and causing the endoplasmic reticulum retention of misfolded glycoprotein as well as components of unassembled oligomeric complexes. The endogenous calnexin knockdown by RNA interference results in an up-regulation of hCLP46 expression and a decrease of Notch intracellular domain expression, indicating the suppression of Notch signaling activation. Calnexin knockdown and dual-luciferase reporter assay experiment indicate that the impairment of interaction between calnexin and hCLP46 weakens Notch signaling activation, but Notch signaling activation in HEK293Trex cell lines induced by tetracycline during different concentrations is not dosage sensitive. Our results suggest that Notch signaling activation is heavily dependent on the interaction between calnexin and hCLP46. Copyright © 2012 John Wiley & Sons, Ltd. |
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Authors:
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Xiaoqin Feng; Lixin Liu |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-4-3 |
Journal Detail:
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Title: Cell biochemistry and function Volume: - ISSN: 1099-0844 ISO Abbreviation: - Publication Date: 2012 Apr |
Date Detail:
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Created Date: 2012-4-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8305874 Medline TA: Cell Biochem Funct Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2012 John Wiley & Sons, Ltd. |
Affiliation:
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Graduate University, Chinese Academy of Sciences, Beijing, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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