Evidence map›Paper›PMID 15163799›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

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

Koki Moriyoshi, Kouichirou Iijima, Hajime Fujii, Hiroshi Ito, Yoshimi Cho, Shigetada Nakanishi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

57 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  17. Review
  18. Regulation of G Protein-Coupled Receptors by Ubiquitination.International journal of molecular sciences · 2017
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Koki MoriyoshiDepartment of Molecular and System Biology, Graduate School of Biostudies, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.
Kouichirou Iijima
Hajime Fujii
Hiroshi Ito
Yoshimi Cho
Shigetada Nakanishi
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

AnimalsBrainCell LineCOS CellsCricetinaeGene ExpressionHumansLysineMiceMice, Inbred C57BLMutagenesis, Site-DirectedNuclear ProteinsProtein Structure, TertiaryReceptor, Metabotropic Glutamate 5Receptors, Metabotropic GlutamateRecombinant ProteinsGRM5 protein, humanGrm5 protein, mouseLysinemetabotropic glutamate receptor type 1Nuclear ProteinsReceptor, Metabotropic Glutamate 5Receptors, Metabotropic GlutamateRecombinant ProteinsRNA, MessengerSeven in Absentia ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID15163799
PMCPMC423243
OpenAlexW2149632214

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.