Evidence map›Paper›PMID 19421138›Full record

ArticleOncogene2009

Fbw7 promotes ubiquitin-dependent degradation of c-Myb: involvement of GSK3-mediated phosphorylation of Thr-572 in mouse c-Myb.

K Kitagawa, Y Hiramatsu, C Uchida, T Isobe, T Hattori, T Oda, K Shibata, S Nakamura, A Kikuchi, M Kitagawa

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.0field-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

37 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  7. Tumor Suppressor FBXW7 and Its Regulation of DNA Damage Response and Repair.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Review
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  11. Review
  12. Article
  13. FBW7 increases drug sensitivity to cisplatin in human nasopharyngeal carcinoma by downregulating the expression of multidrug resistance-associated protein.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  14. Article
  15. Article
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  17. Article
  18. Review
  19. 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

10 authors at 3 institutions in 2 countries.

K KitagawaDepartment of Biochemistry 1, Hamamatsu University School of Medicine, Higashi-ku, Hamamatsu, Shizuoka, Japan. kitamasa@hama-med.ac.jp
Y Hiramatsu
C Uchida
T Isobe
T Hattori
T Oda
K Shibata
S Nakamura
A Kikuchi
M Kitagawa
Hamamatsu University School of Medicine · JPNational University of Singapore · SGHiroshima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of oncoprotein c-Myb oscillates during hematopoiesis and hematological malignancies. Its quantity is not only regulated through transcriptional control but also through the ubiquitin-proteasome pathway, accompanied by phosphorylation, although the mechanisms are poorly understood. In this report, we tried to identify an E3 ubiquitin ligase, which targets c-Myb for ubiquitin-dependent degradation. We found that an F-box protein, Fbw7, interacted with c-Myb, which is mutated in numerous cancers. Fbw7 facilitated ubiquitylation and degradation of c-Myb in intact cells. Moreover, depletion of Fbw7 by RNA interference delayed turnover and increased the abundance of c-Myb in myeloid leukemia cells concomitantly, and suppressed the transcriptional level of gamma-globin, which receives transcriptional repression from c-Myb. In addition, we analysed sites required for both ubiquitylation and degradation of c-Myb. We found that Thr-572 is critical for Fbw7-mediated ubiquitylation in mouse c-Myb using site-directed mutagenesis. Fbw7 recognized the phosphorylation of Thr-572, which was mediated by glycogen synthase kinase 3 (GSK3). In consequence, the c-Myb protein was markedly stabilized by the substitution of Thr-572 to Ala. These observations suggest that SCF(Fbw7) ubiquitin ligase regulates phosphorylation-dependent degradation of c-Myb protein.

Indexed as

AnimalsCell Cycle ProteinsCells, CulturedF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Glycogen Synthase Kinase 3HumansImmunoprecipitationMiceMutagenesis, Site-DirectedPhosphorylationProto-Oncogene Proteins c-mybProto-Oncogene Proteins c-mycReceptor, Notch1Reverse Transcriptase Polymerase Chain ReactionRNA, MessengerCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanGlycogen Synthase Kinase 3Myc protein, mouseNotch1 protein, mouseProto-Oncogene Proteins c-mybProto-Oncogene Proteins c-mycReceptor, Notch1RNA, MessengerThreonineUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID19421138
OpenAlexW1992150326

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.