Evidence map›Paper›PMID 8861945›Full record

ArticleThe EMBO journal1996

The receptor-associated protein (RAP) binds calmodulin and is phosphorylated by calmodulin-dependent kinase II.

C M Petersen, L Ellgaard, A Nykjaer, F Vilhardt, H Vorum, H C Thøgersen, M S Nielsen, C Jacobsen, S K Moestrup, J Gliemann

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

9 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  7. Article
  8. Article
  9. The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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

10 authors at 1 institution in 1 country.

C M PetersenDepartment of Medical Biochemistry, University of Aarhus, Denmark.
L Ellgaard
A Nykjaer
F Vilhardt
H Vorum
H C Thøgersen
M S Nielsen
C Jacobsen
S K Moestrup
J Gliemann
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The receptor-associated protein, RAP, is an intracellular protein that may function as a chaperone for the LDL-receptor family receptors. Here we report calmodulin as the first identified RAP binding protein outside of the LDL-receptor family members. We demonstrate that RAP binds calmodulin in a Ca2+- and pH-dependent manner characteristic of calmodulin-dependent enzymes, and present evidence that RAP is a substrate for calmodulin-dependent enzymes. Thus, CaM-kinase II and calcineurin readily phosphorylate and dephosphorylate, respectively, serine residues in RAP, and in the individual RAP domains D2 (amino acids 113-218) and D3 (amino acids 219-323) which both contain sites for CaM-kinase II-mediated phosphorylation and for calmodulin binding. In addition, we provide evidence that RAP is phosphorylated by other kinases such as casein kinase II. Studies of 32[ortho]P-labelled cell cultures demonstrate that RAP is phosphorylated in vivo. Our results suggest that RAP may have hitherto unknown functions implicating phosphorylation and calmodulin-mediated modulation.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCalcineurinCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCalmodulin-Binding ProteinsCarrier ProteinsCasein Kinase IIGlycoproteinsHydrogen-Ion ConcentrationLDL-Receptor Related Protein-Associated ProteinMolecular Sequence DataPhosphoprotein PhosphatasesPhosphorylationCalcineurinCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCalmodulin-Binding ProteinsCarrier ProteinsCasein Kinase IIGlycoproteinsLDL-Receptor Related Protein-Associated ProteinPhosphoprotein PhosphatasesPhosphoserineProtein Serine-Threonine KinasesReceptors, LDLRecombinant Fusion Proteins

Identifiers

PMID8861945
PMCPMC452140
OpenAlexW31022410

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.