Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin.

Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Research Abstract Details 

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Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Abstract Text:

Ying Huang,Jun-ichi Niwa,Gen Sobue,Gerda E Breitwieser,

Calcium-sensing receptors (CaR) contribute to regulation of systemic calcium homeostasis by activation of G(q)- and G(i)-linked signaling pathways in the parathyroids, kidney, and intestine. Little is known about the mechanisms regulating CaR synthesis and degradation. Screening of a human kidney yeast two-hybrid library identified the E3 ubiquitin ligase dorfin as a binding partner for the intracellular carboxyl terminus of CaR. Interaction between CaR and dorfin was confirmed by coimmunoprecipitation from HEK293 cells. Ubiquitination of CaR was observed in the presence of the proteasomal inhibitor MG132; mutation of all putative intracellular loop and carboxyl-terminal lysine residues abolished ubiquitination of CaR. Coexpression with dorfin decreased the amount of total CaR protein and increased CaR ubiquitination, whereas a dominant negative fragment of dorfin had opposite effects. The AAA-ATPase p97/valosin-containing protein associates with both CaR and dorfin in HEK293 cells. Treatment with tunicamycin, an inhibitor of N-linked glycosylation, induced the appearance of the unglycosylated 115-kDa CaR form, which was further increased by exposure to MG132, or upon transfection with a dorfin dominant negative construct, suggesting that dorfin-mediated proteasomal degradation of immature CaR occurs from the endoplasmic reticulum. Because endogenous CaR in Madin-Darby canine kidney cells is also subject to degradation from the endoplasmic reticulum, dorfin-mediated ubiquitination may contribute to a general mechanism for CaR quality control during biosynthesis.

Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Publishing Authors By Initials

Y Huang,J Niwa,G Sobue,GE Breitwieser,

For similar enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research abstracts see: enzymes and coenzymes: enzymes: ligases: ubiquitin-protein ligase complexes: ubiquitin-protein ligases research

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Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 11610-7

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 2

MONTH: 03

YEAR: 2006

Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Keywords Mesh Terms:

KEYWORDS: Ubiquitin-Protein Ligases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin. Information

Substance Name: Ubiquitin-Protein Ligases

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin.

AFFILIATION: Department of Biology, Syracuse University, Syracuse, New York 13244, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM58578

ACRONYM: GM

MEDLINETA: J Biol Chem

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