Evidence map›Paper›PMID 14517323›Full record

ArticleMolecular biology of the cell2003

The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus.

Margarita Cabrera, Manuel Muñiz, Josefina Hidalgo, Lucia Vega, María Esther Martín, Angel Velasco

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

43 citing papers in PubMed, 134 citations in OpenAlex.

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  15. A modified cholera toxin B subunit containing an ER retention motif enhances colon epithelial repairFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  16. Review
  17. The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019
    Review
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  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Margarita CabreraDepartment of Cell Biology, Faculty of Biology, University of Seville, 41012 Seville, Spain.
Manuel Muñiz
Josefina Hidalgo
Lucia Vega
María Esther Martín
Angel Velasco
Universidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The KDEL receptor is a Golgi/intermediate compartment-located integral membrane protein that carries out the retrieval of escaped ER proteins bearing a C-terminal KDEL sequence. This occurs throughout retrograde traffic mediated by COPI-coated transport carriers. The role of the C-terminal cytoplasmic domain of the KDEL receptor in this process has been investigated. Deletion of this domain did not affect receptor subcellular localization although cells expressing this truncated form of the receptor failed to retain KDEL ligands intracellularly. Permeabilized cells incubated with ATP and GTP exhibited tubular processes-mediated redistribution from the Golgi area to the ER of the wild-type receptor, whereas the truncated form lacking the C-terminal domain remained concentrated in the Golgi. As revealed with a peptide-binding assay, this domain did not interact with both coatomer and ARF-GAP unless serine 209 was mutated to aspartic acid. In contrast, alanine replacement of serine 209 inhibited coatomer/ARF-GAP recruitment, receptor redistribution into the ER, and intracellular retention of KDEL ligands. Serine 209 was phosphorylated by both cytosolic and recombinant protein kinase A (PKA) catalytic subunit. Inhibition of endogenous PKA activity with H89 blocked Golgi-ER transport of the native receptor but did not affect redistribution to the ER of a mutated form bearing aspartic acid at position 209. We conclude that PKA phosphorylation of serine 209 is required for the retrograde transport of the KDEL receptor from the Golgi complex to the ER from which the retrieval of proteins bearing the KDEL signal depends.

Indexed as

SulfonamidesAdenosine TriphosphateADP-Ribosylation FactorsAnimalsAspartic AcidCell CompartmentationCells, CulturedChlorocebus aethiopsCloning, MolecularCOS CellsCyclic AMP-Dependent Protein KinasesEndoplasmic ReticulumFluorescent Antibody TechniqueGolgi ApparatusGTPase-Activating ProteinsGuanosine TriphosphateAdenosine TriphosphateADP-Ribosylation FactorsAspartic AcidCyclic AMP-Dependent Protein KinasesGTPase-Activating ProteinsGuanosine TriphosphateIsoquinolinesKDEL receptorN-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamideReceptors, PeptideSerineSulfonamides

Identifiers

PMID14517323
PMCPMC207004
OpenAlexW2103001017

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.