Oncogenic MAGEA-TRIM28 ubiquitin ligase downregulates autophagy by ubiquitinating and degrading AMPK in cancer

Carlos T. Pineda, Patrick Ryan Potts

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Autophagy is commonly altered in cancer and has a complicated, but important role in regulation of tumor growth. Autophagy is often tumor suppressive in the early stages of cancer development, but contributes to the late stages of tumor growth. Because of this, putative oncogenes that modulate autophagy signaling are especially interesting. Here we discuss our recent work detailing the function of the MAGEATRIM28 ubiquitin ligase as an oncogene product that targets PRKAA1/AMPKa1 for ubiquitination and proteasome-mediated degradation. Degradation of AMPK, a master cellular energy sensor and regulator, by MAGEA-TRIM28 results in significantly reduced autophagy and changes in cellular metabolism, including upregulation of MTOR signaling. Overall, expression of MAGEA3 (or MAGEA6) and degradation of AMPK is sufficient to induce transformation of normal cells and promote multiple hallmarks of cancer.

Original languageEnglish (US)
Pages (from-to)844-846
Number of pages3
JournalAutophagy
Volume11
Issue number5
DOIs
StatePublished - Jan 1 2015

Fingerprint

AMP-Activated Protein Kinases
Autophagy
Ligases
Ubiquitin
Down-Regulation
Neoplasms
Ubiquitination
Oncogene Proteins
Proteasome Endopeptidase Complex
Growth
Oncogenes
Up-Regulation

Keywords

  • AMPK
  • Autophagy
  • Cancer
  • KAP1
  • MAGE
  • Melanoma-antigen
  • Spermatogenesis
  • Testis
  • TRIM28
  • Ubiquitin

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Oncogenic MAGEA-TRIM28 ubiquitin ligase downregulates autophagy by ubiquitinating and degrading AMPK in cancer. / Pineda, Carlos T.; Potts, Patrick Ryan.

In: Autophagy, Vol. 11, No. 5, 01.01.2015, p. 844-846.

Research output: Contribution to journalArticle

Pineda, Carlos T. ; Potts, Patrick Ryan. / Oncogenic MAGEA-TRIM28 ubiquitin ligase downregulates autophagy by ubiquitinating and degrading AMPK in cancer. In: Autophagy. 2015 ; Vol. 11, No. 5. pp. 844-846.
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