Evidence map›Paper›PMID 15021906›Full record

ArticleOncogene2004

Multiple cell-type-specific elements regulate Myc protein stability.

Andreas Herbst, Simone E Salghetti, So Young Kim, William P Tansey

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2004. 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. c-Myc: an emerging participant in heart failure.Frontiers in cardiovascular medicine · 2026
    Review
  2. Review
  3. Review
  4. Co-Operativity between MYC and BCL-2 Pro-Survival Proteins in Cancer.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Recent advances in searching c-Myc transcriptional cofactors during tumorigenesis.Journal of experimental & clinical cancer research : CR · 2018
    Review
  7. Review
  8. Article
  9. Therapeutic strategies to inhibit MYC.Cold Spring Harbor perspectives in medicine · 2014
    Review
  10. MYC degradation.Cold Spring Harbor perspectives in medicine · 2014
    Review
  11. An overview of MYC and its interactome.Cold Spring Harbor perspectives in medicine · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. WWP1: a versatile ubiquitin E3 ligase in signaling and diseases.Cellular and molecular life sciences : CMLS · 2012
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors.

Andreas HerbstCold Spring Harbor Laboratory, 1 Bungtown Rd, PO Box 100, Cold Spring Harbor, NY 11724, USA.
Simone E Salghetti
So Young Kim
William P Tansey

Funding

Single-Cell Biology Shared ResourceP30CA045508 · NCI · COLD SPRING HARBOR LABORATORY · PI John Edward Moses · 1987 to 2026
$118.9M
VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
NCI NIH HHS CA-13106NCI NIH HHS CA45508
6 · The paper itself

Abstract

Myc is a highly unstable transcription factor that is destroyed by ubiquitin (Ub)-mediated proteolysis. We have previously identified an amino-terminal 'degron' within Myc that signals its destruction; this degron spans the transcriptional activation domain of Myc, and includes two highly conserved regions called Myc boxes I and II. We now report the identification of a second element--the D-element--which is also required for Myc proteolysis. The centrally located D-element is distinct from the PEST domain in Myc, but includes Myc box III, a third highly conserved region with no previously known function. We show that deletion of the D-element stabilizes the Myc protein without affecting its ubiquitylation, and report that the D-element and the degron act in a cell-type-specific manner to direct Myc proteolysis. These data thus demonstrate that Myc stability is regulated at both the ubiquitylation and postubiquitylation levels, and reveal that substrates of the Ub-proteasome system can be targeted for destruction differently in different cell types.

Indexed as

Amino Acid SequenceAnimalsConserved SequenceCysteine EndopeptidasesHumansMolecular Sequence DataMultienzyme ComplexesProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mycRatsUbiquitinCysteine EndopeptidasesMultienzyme ComplexesProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mycUbiquitin

Identifiers

PMID15021906

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.