Evidence map›Paper›PMID 21280599›Full record

ArticleBiochemistry2011

Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an α-helix.

Maxim V Dorovkov, Alla S Kostyukova, Alexey G Ryazanov

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Annexin, a Protein for All Seasons: From Calcium Dependent Membrane Metabolism to RNA Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  5. Unlocking TRPM7 interactions: A database-driven quest.Computational and structural biotechnology journal · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Conformational Changes of Anoplin, W-MreBInternational journal of molecular sciences · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Mibefradil represents a new class of benzimidazole TRPM7 channel agonists.Pflugers Archiv : European journal of physiology · 2016
    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

3 authors at 1 institution in 1 country.

Maxim V DorovkovDepartment of Pharmacology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, United States. dorovkma@umdnj.edu
Alla S Kostyukova
Alexey G Ryazanov
Rutgers, The State University of New Jersey · US

Funding

Regulation of Metal Ion Homeostasis by Channel KinasesP01GM078195 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI STOKES, JOHN B · 2007 to 2011
$8.7M
NIGMS NIH HHS P01 GM078195
6 · The paper itself

Abstract

TRPM7 is an unusual bifunctional protein consisting of an α-kinase domain fused to a TRP ion channel. Previously, we have identified annexin A1 as a substrate for TRPM7 kinase and found that TRPM7 phosphorylates annexin A1 at Ser5 within the N-terminal α-helix. Annexin A1 is a Ca(2+)-dependent membrane binding protein, which has been implicated in membrane trafficking and reorganization. The N-terminal tail of annexin A1 can interact with either membranes or S100A11 protein, and it adopts the conformation of an amphipathic α-helix upon these interactions. Moreover, the existing evidence indicates that the formation of an α-helix is essential for these interactions. Here we show that phosphorylation at Ser5 prevents the N-terminal peptide of annexin A1 from adopting an α-helical conformation in the presence of membrane-mimetic micelles as well as phospholipid vesicles. We also show that phosphorylation at Ser5 dramatically weakens the binding of the peptide to S100A11. Our data suggest that phosphorylation at Ser5 regulates the interaction of annexin A1 with membranes as well as S100A11 protein.

Indexed as

Amino Acid SequenceAnimalsAnnexin A1Cell MembraneMolecular Sequence DataPeptide FragmentsPhosphorylationProtein Structure, SecondaryS100 ProteinsSerineTRPM Cation ChannelsAnnexin A1Peptide FragmentsS100 ProteinsSerineTRPM Cation Channels

Identifiers

PMID21280599
PMCPMC3062375
OpenAlexW2069426484

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.