Evidence map›Paper›PMID 8830770›Full record

ArticleThe Journal of cell biology1996

Protein kinase C mu is located at the Golgi compartment.

J Prestle, K Pfizenmaier, J Brenner, F J Johannes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
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  9. Regulation of Golgi structure and secretion by receptor-induced G protein βγ complex translocation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
  11. Remodeling of the Golgi structure by ERK signaling.Communicative & integrative biology · 2009
    Article
  12. Article
  13. Protein kinase D1: a new component in TLR9 signaling.Journal of immunology (Baltimore, Md. : 1950) · 2008
    Article
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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

4 authors at 1 institution in 1 country.

J PrestleInstitute of Cell Biology and Immunology, University of Stuttgart, Germany.
K Pfizenmaier
J Brenner
F J Johannes
University of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase C mu (PKC mu) displays unusual structural features like a pleckstrin homology domain and an amino-terminal hydrophobic region with a putative leader peptide and transmembrane sequence. As a discrete location often is a direct clue to the potential biological function of a kinase, antibodies directed against unique amino- and carboxy-terminal domains of PKC mu were used to localize the protein within intracellular compartments in immunofluorescence and subcellular fractionation studies. Confocal laser scanning microscopy showed colocalization of PKC mu with the resident Golgi marker protein beta 1,4 galactosyltransferase in PKC mu transfectants and in the human hepatocellular carcinoma cell line HepG2, expressing endogenous PKC mu. Long-term treatment of cells with brefeldin A, which disintegrates the Golgi apparatus, disrupted PKC mu-specific staining. Cosegregation of PKC mu with beta 1,4 galactosyltransferase, but not with the endosomal marker rab5, upon density gradient fractionation and Western blot analysis of HepG2 cell extracts, provides independent evidence for a Golgi localization of PKC mu. Moreover, cellular sulfate uptake and Golgi-specific glycosaminoglycan sulfation was enhanced in PKC mu transfectants. Together, these data suggest that PKC mu is a resident protein kinase of the core Golgi compartment and is involved in basal transport processes.

Indexed as

3T3 CellsAnimalsAntibody SpecificityBlotting, NorthernCHO CellsCricetinaeFluorescent Antibody Technique, IndirectGalactosyltransferasesGlycosaminoglycansGolgi ApparatusHeLa CellsHumansIsoenzymesMiceMicroscopy, ConfocalProtein Kinase CGalactosyltransferasesGlycosaminoglycansIsoenzymesProtein Kinase CRNA, MessengerSulfates

Identifiers

PMID8830770
PMCPMC2121004
OpenAlexW2040263555

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.