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  Seven in absentia homolog 1A mediates ubiquitination and degradation of group 1 metabotropic glutamate receptors

Moriyoshi, K., Iijima, K., Fujii, H., Ito, H., Cho, Y., & Nakanishi, S. (2004). Seven in absentia homolog 1A mediates ubiquitination and degradation of group 1 metabotropic glutamate receptors. Proc Natl Acad Sci U S A, 101(23), 8614-9. doi:10.1073/pnas.0403042101.

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https://www.ncbi.nlm.nih.gov/pubmed/15163799 (beliebiger Volltext)
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 Urheber:
Moriyoshi, K., Autor
Iijima, K., Autor
Fujii, H., Autor
Ito, Hiroshi1, Autor           
Cho, Y., Autor
Nakanishi, S., Autor
Affiliations:
1Memory and Navigation Circuits Group, Max Planck Institute for Brain Research, Max Planck Society, ou_2461699              

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Schlagwörter: Animals Brain/metabolism COS Cells Cell Line Cricetinae Gene Expression Humans Lysine/chemistry Mice Mice, Inbred C57BL Mutagenesis, Site-Directed Nuclear Proteins/chemistry/genetics/*metabolism Protein Structure, Tertiary RNA, Messenger/genetics/metabolism Receptor, Metabotropic Glutamate 5 Receptors, Metabotropic Glutamate/chemistry/genetics/*metabolism Recombinant Proteins/chemistry/genetics/metabolism Ubiquitin/metabolism Ubiquitin-Protein Ligases
 Zusammenfassung: Seven in absentia homolog 1A (Siah1A) is a member of the RING-finger-containing E3 ubiquitin ligases and has been shown to bind to the Siah-interacting domain (SID) at the carboxyl-terminal tails of the long splice forms of group 1 metabotropic glutamate receptors (mGluR1a and mGluR5). We examined the function of Siah1A in ubiquitination and degradation of group 1 mGluRs in heterologously expressing cell lines. Coexpression of Siah1A markedly decreased the SID-containing splice forms of group 1 mGluRs but not the SID-lacking mGluR1b splice form or the SID-deleted mGluR1a mutant. The decrease of mGluR1a resulted from accelerated protein turnover, as revealed by pulse-chase experiments. The Siah1A-mediated degradation of group 1 mGluRs was abrogated by not only mutations at the RING-finger domain of Siah1A but also treatment with a proteasome inhibitor. Siah1A coexpression induced strong ubiquitination of group 1 mGluRs. Replacements of lysine residues with arginine showed that Siah1A-mediated ubiquitination occurs at multiple lysine residues spanning both the seven-transmembrane region and carboxyl-terminal tail of mGluR5. In situ hybridization histochemistry showed a wide-spread distribution of Siah1 mRNAs, with high expression in the hippocampal pyramidal neurons and cerebellar Purkinje cells. Group 1 mGluRs play critical roles in the neural plasticity in both the hippocampal neurons and Purkinje cells. This investigation indicates that Siah1A serves as a selective ubiquitin ligase that mediates ubiquitination-dependent degradation of long splice variants of group 1 mGluRs and would contribute to posttranslational down-regulation of group 1 mGluRs.

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 Datum: 2004
 Publikationsstatus: Erschienen
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 Identifikatoren: Anderer: 15163799
DOI: 10.1073/pnas.0403042101
ISSN: 0027-8424 (Print)0027-8424 (Linking)
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Titel: Proc Natl Acad Sci U S A
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 101 (23) Artikelnummer: - Start- / Endseite: 8614 - 9 Identifikator: -