Evidence map›Paper›PMID 15987778›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Phosphorylation-regulated endoplasmic reticulum retention signal in the renal outer-medullary K+ channel (ROMK).

Anthony D O'Connell, Qiang Leng, Ke Dong, Gordon G MacGregor, Gerhard Giebisch, Steven C Hebert

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. KCNJ1 inhibits tumor proliferation and metastasis and is a prognostic factor in clear cell renal cell carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  7. Distal convoluted tubule.Clinical journal of the American Society of Nephrology : CJASN · 2014
    Review
  8. MicroRNA-194 (miR-194) regulates ROMK channel activity by targeting intersectin 1.American journal of physiology. Renal physiology · 2014
    Article
  9. Article
  10. Regulation of potassium channel trafficking in the distal nephron.Current opinion in nephrology and hypertension · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. MicroRNA 802 stimulates ROMK channels by suppressing caveolin-1.Journal of the American Society of Nephrology : JASN · 2011
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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.

Anthony D O'ConnellDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520.
Qiang Leng
Ke Dong
Gordon G MacGregor
Gerhard Giebisch
Steven C Hebert
Yale University · US

Funding

STRUCTURE AND FUNCTION OF ROMK CHANNEL IN KIDNEYR01DK054999 · NIDDK · YALE UNIVERSITY · PI WANG, TONG WANG · 2001 to 2008
$3.2M
ROMK CHANNEL FUNCTION AND REGULATION IN KIDNEYR01DK054998 · NIDDK · YALE UNIVERSITY · PI GIEBISCH, GERHARD H · 1999 to 2003
$883k
NIDDK NIH HHS DK 54998NIDDK NIH HHS DK 54999NIDDK NIH HHS R01 DK054998NIDDK NIH HHS R01 DK054999
6 · The paper itself

Abstract

The renal outer-medullary K+ channel (ROMK; Kir1.1) mediates K+ secretion in the renal mammalian nephron that is critical to both sodium and potassium homeostasis. The posttranscriptional expression of ROMK in the plasma membrane of cells is regulated by delivery of protein from endoplasmic reticulum (ER) to the cell surface and by retrieval by dynamin-dependent endocytic mechanisms in clathrin-coated pits. The S44 in the NH(2) terminus of ROMK1 can be phosphorylated by PKA and serum- and glucocorticoid-inducible kinase-1, and this process increases surface expression of functional channels. We present evidence that phosphorylation of S44 modulates channel expression by increasing its cell surface delivery consequent to suppression of a COOH-terminal ER retention signal. This phosphorylation switch of the ER retention signal could provide a pool of mature and properly folded channels for rapid delivery to the plasma membrane. The x-ray crystal structures of inward rectifier K+ channels have shown a close apposition of the NH(2) terminus with the distal COOH terminus of the adjacent subunit in the channel homotetramer, which is important to channel gating. Thus, NH(2)-terminal phosphorylation modifying a COOH-terminal ER retention signal in ROMK1 could serve as a checkpoint for proper subunit folding critical to channel gating.

Indexed as

AnimalsBlotting, WesternCloning, MolecularEndoplasmic ReticulumGreen Fluorescent ProteinsHumansHydrogen-Ion ConcentrationIon Channel GatingMicroscopy, ConfocalMutagenesis, Site-DirectedOocytesPatch-Clamp TechniquesPhosphorylationPotassium Channels, Inwardly RectifyingProtein TransportSignal Transductionenhanced green fluorescent proteinGreen Fluorescent ProteinsKCNJ1 protein, humanPotassium Channels, Inwardly Rectifying

Identifiers

PMID15987778
PMCPMC1175014
OpenAlexW2039456047

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.