Evidence map›Paper›PMID 9362517›Full record

ArticleThe Journal of cell biology1997

Constitutive proteolysis of the ErbB-4 receptor tyrosine kinase by a unique, sequential mechanism.

M Vecchi, G Carpenter

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-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

36 citing papers in PubMed, 115 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. An iron-regulated and glycosylation-dependent proteasomal degradation pathway for the plasma membrane metal transporter ZIP14.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Sequential proteolytic processing of an interferon-alpha receptor subunit by TNF-alpha converting enzyme and presenilins.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2012
    Article
  11. WWP1: a versatile ubiquitin E3 ligase in signaling and diseases.Cellular and molecular life sciences : CMLS · 2012
    Review
  12. Article
  13. Article
  14. A nuclear variant of ErbB3 receptor tyrosine kinase regulates ezrin distribution and Schwann cell myelination.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  15. Article
  16. MUC1 is a substrate for gamma-secretase.Journal of cellular biochemistry · 2009
    Article
  17. Article
  18. Review
  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

2 authors at 1 institution in 1 country.

M VecchiDepartment of Biochemistry and Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA.
G Carpenter
Vanderbilt University · US

Funding

STUDIES OF THE RECEPTOR FOR EPIDERMAN GROWTH FACTORR01CA024071 · NCI · VANDERBILT UNIVERSITY · PI CARPENTER, GRAHAM F · 1985 to 2001
$407k
NCI NIH HHS CA24071
6 · The paper itself

Abstract

The heregulin receptor tyrosine kinase ErbB-4 is constitutively cleaved, in the presence or absence of ligand, by an exofacial proteolytic activity producing a membrane-anchored cytoplasmic domain fragment of 80 kD. Based on selective sensitivity to inhibitors, the proteolytic activity is identified as that of a metalloprotease. The 80-kD product is tyrosine phosphorylated and retains tyrosine kinase activity. Importantly, the levels of this fragment are controlled by proteasome function. When proteasome activity is inhibited for 6 h, the kinase-active 80-kD ErbB-4 fragment accumulates to a level equivalent to 60% of the initial amount of native ErbB-4 (approximately 10(6) receptors per cell). Hence, proteasome activity is essential to prevent the accumulation of a significant level of ligand-independent, active ErbB-4 tyrosine kinase generated by metalloprotease activity. Proteasome activity, however, does not act on the native ErbB-4 receptor before the metalloprotease-mediated cleavage, as no ErbB-4 fragments accumulate when metalloprotease activity is blocked. Although no ubiquitination of the native ErbB-4 is detected, the 80-kD fragment is polyubiquitinated. The data, therefore, describe a unique pathway for the processing of growth factor receptors, which involves the sequential function of an exofacial metalloprotease and the cytoplasmic proteasome.

Indexed as

3T3 CellsAnimalsCysteine EndopeptidasesEnzyme ActivationErbB ReceptorsHumansHydrolysisMetalloendopeptidasesMiceMolecular WeightMultienzyme ComplexesPeptide FragmentsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalReceptor, ErbB-4UbiquitinsCysteine EndopeptidasesERBB4 protein, humanErbb4 protein, mouseErbB ReceptorsMetalloendopeptidasesMultienzyme ComplexesPeptide FragmentsProteasome Endopeptidase ComplexReceptor, ErbB-4Ubiquitins

Identifiers

PMID9362517
PMCPMC2139967
OpenAlexW2088035322

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.