Evidence map›Paper›PMID 19270695›Full record

ArticleNature cell biology2009

Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction.

Daming Gao, Hiroyuki Inuzuka, Alan Tseng, Rebecca Y Chin, Alex Toker, Wenyi Wei

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

166 citing papers in PubMed, 276 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. E3 ubiquitin ligase SKP2 limits autophagosome formation duringFrontiers in cellular and infection microbiology · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Oncology reports · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. FOXO transcription factors as mediators of stress adaptation.Nature reviews. Molecular cell biology · 2024
    Review

106 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Daming GaoDepartment of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
Hiroyuki Inuzuka
Alan Tseng
Rebecca Y Chin
Alex Toker
Wenyi Wei
Beth Israel Deaconess Medical Center · US

Funding

The RBP2/JARID1A/KDM5A Histone Demethylase as a Potential Drug Target in CancerR01CA076120 · NCI · DANA-FARBER CANCER INSTITUTE · PI KAELIN, WILLIAM G. · 1998 to 2015
$3.6M
Interplay between Cdh1 and major regulatory pathways in human cancerR01GM089763 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WEI, WENYI · 2009 to 2018
$3.0M
The Akt and NFAT Pathway and the Regulaton of Cancer Cell MotilityR01CA122099 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI TOKER, ALEX · 2007 to 2011
$1.4M
NCI NIH HHS CA076120NCI NIH HHS CA122099NCI NIH HHS R01 CA076120NCI NIH HHS R01 CA122099NIGMS NIH HHS R01 GM089763
6 · The paper itself

Abstract

Deregulated Skp2 function promotes cell transformation, and this is consistent with observations of Skp2 overexpression in many human cancers. However, the mechanisms underlying elevated Skp2 expression are still unknown. Here we show that the serine/threonine protein kinase Akt1, but not Akt2, directly controls Skp2 stability by a mechanism that involves degradation by the APC-Cdh1 ubiquitin ligase complex. We show further that Akt1 phosphorylates Skp2 at Ser 72, which is required to disrupt the interaction between Cdh1 and Skp2. In addition, we show that Ser 72 is localized within a putative nuclear localization sequence and that phosphorylation of Ser 72 by Akt leads to cytoplasmic translocation of Skp2. This finding expands our knowledge of how specific signalling kinase cascades influence proteolysis governed by APC-Cdh1 complexes, and provides evidence that elevated Akt activity and cytoplasmic Skp2 expression may be causative for cancer progression.

Indexed as

Amino Acid SequenceAnaphase-Promoting Complex-CyclosomeAnimalsCasein Kinase ICytoplasmHeLa CellsHumansMiceMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphorylationPhosphoserineProtein BindingProtein Processing, Post-TranslationalProtein StabilityProtein TransportAnaphase-Promoting Complex-CyclosomeCasein Kinase IPhosphatidylinositol 3-KinasesPhosphoserineProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanS-Phase Kinase-Associated ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID19270695
PMCPMC2910589
OpenAlexW2073452121

What OpenQuestion holds

Textmetadata
LicenceTDM
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.