Evidence map›Paper›PMID 12217858›Full record

ArticleAmerican journal of physiology. Renal physiology2002

K depletion increases protein tyrosine kinase-mediated phosphorylation of ROMK.

Dao-Hong Lin, Hyacinth Sterling, Kenneth M Lerea, Paul Welling, Lianhong Jin, Gerhard Giebisch, Wen-Hui Wang

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Renal physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Mechanistic target of rapamycin complex-1 plays a role in inhibiting kidney KAmerican journal of physiology. Renal physiology · 2026
    Article
  2. Control of sodium and potassium homeostasis by renal distal convoluted tubules.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2023
    Article
  3. Role of WNK4 and kidney-specific WNK1 in mediating the effect of high dietary KAmerican journal of physiology. Renal physiology · 2018
    Article
  4. Article
  5. Src-family protein tyrosine kinase phosphorylates WNK4 and modulates its inhibitory effect on KCNJ1 (ROMK).Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Distal convoluted tubule.Comprehensive Physiology · 2015
    Review
  7. MicroRNA-194 (miR-194) regulates ROMK channel activity by targeting intersectin 1.American journal of physiology. Renal physiology · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Src family protein tyrosine kinase (PTK) modulates the effect of SGK1 and WNK4 on ROMK channels.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Regulation of potassium (K) handling in the renal collecting duct.Pflugers Archiv : European journal of physiology · 2009
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

7 authors at 4 institutions in 2 countries.

Dao-Hong LinDepartment of Pharmacology, New York Medical College, Valhalla 10595, USA.
Hyacinth Sterling
Kenneth M Lerea
Paul Welling
Lianhong Jin
Gerhard Giebisch
Wen-Hui Wang
Harbin Medical University · CNNew York Medical College · USUniversity of Maryland, Baltimore · USYale University · US

Funding

Role of Kir4.1 in Regulating NCC and ROMK in DCTR01DK054983 · NIDDK · NEW YORK MEDICAL COLLEGE · PI ELLISON, DAVID H, WANG, WENHUI · 2001 to 2020
$7.4M
MODULATION OF K+ CHANNELS IN RENAL COLLECTING DUCTR01DK047402 · NIDDK · NEW YORK MEDICAL COLLEGE · PI WANG, WENHUI · 1999 to 2007
$2.3M
Role of Kir4.1 in Regulating NCC and ROMK in DCTR56DK054983 · NIDDK · NEW YORK MEDICAL COLLEGE · PI ELLISON, DAVID H, WANG, WENHUI · 2021 to 2021
$100k
MODULATION OF K+ CHANNELS IN RENAL COLLECTING DUCTR29DK047402 · NIDDK · NEW YORK MEDICAL COLLEGE · PI WANG, WEN-HUI · 1994 to 1998
–
NIDDK NIH HHS DK-47402NIDDK NIH HHS DK-54983NIDDK NIH HHS R01 DK047402NIDDK NIH HHS R01 DK054983NIDDK NIH HHS R56 DK054983
6 · The paper itself

Abstract

We purified His-tagged ROMK1 and carried out in vitro phosphorylation assays with (32)P-radiolabeled ATP to determine whether ROMK1 protein is a substrate for PTK. Addition of active c-Src and [(32)P]ATP to the purified ROMK1 protein resulted in the phosphorylation of the ROMK1 protein. However, c-Src did not phosphorylate R1Y337A in which tyrosine residue 337 was mutated to alanine. Furthermore, phosphopeptide mapping identified two phosphopeptides from the trypsin-digested ROMK1 protein. In contrast, no phosphorylated peptide has been found in the trypsin-digested R1Y337A protein. This suggested that two phosphorylated peptides might contain the same tyrosine residue. Also, addition of c-Src and [(32)P]ATP phosphorylated the synthesized peptide corresponding to amino acid sequence 333-362 of the COOH terminus of ROMK1. We then examined the effect of dietary K intake on the tyrosine-phosphorylated ROMK level. Although the ROMK channels pulled down by immunoprecipitation with ROMK antibody were the same from rats on a K-deficient diet or on a high-K diet, more ROMK channels were phosphorylated by PTK in rats on a K-deficient diet than those on a high-K diet. We conclude that ROMK1 can be phosphorylated by PTK and that tyrosine residue 337 is the key site for the phosphorylation. Also, the tyrosine phosphorylation of ROMK is modulated by dietary K intake. This strongly suggests that PTK is an important member of the aldosterone-independent signal transduction pathway for regulating renal K secretion.

Indexed as

Potassium Channels, Inwardly RectifyingAmino Acid SequenceAnimalsBlotting, WesternDNAFemaleMalePeptide MappingPhosphopeptidesPhosphorylationPotassiumPotassium ChannelsPotassium, DietaryPrecipitin TestsProtein-Tyrosine KinasesRatsDNAKcnj1 protein, ratPhosphopeptidesPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingPotassium, DietaryProtein-Tyrosine KinasesRecombinant ProteinsTyrosine

Identifiers

PMID12217858
PMCPMC2843414
OpenAlexW2168785337

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.