Oncosuppressive functions of autophagy

Eugenia Morselli, Lorenzo Galluzzi, Oliver Kepp, Guillermo Mariño, Mickael Michaud, Ilio Vitale, Maria Chiara Maiuri, Guido Kroemer

Research output: Contribution to journalArticlepeer-review


Macroautophagy (herein referred to as autophagy) constitutes a phylogenetically old mechanism leading to the lysosomal degradation of cytoplasmic structures. At baseline levels, autophagy exerts homeostatic functions by ensuring the turnover of potentially harmful organelles and long-lived aggregate-prone proteins. Moreover, the autophagic flow can be dramatically upregulated in response to a plethora of stressful conditions, including glucose, amino acid, oxygen, or growth factor deprivation, accumulation of unfolded proteins in the endoplasmic reticulum, and invasion by intracellular pathogens. In some experimental settings, stress-induced autophagy has been shown to contribute to programmed cell death. Nevertheless, autophagy most often confers cytoprotection by providing cells with new metabolic substrates or by ridding them of noxious intracellular entities including protein aggregates and invading organisms. Thus, autophagy has been implicated in an ever-increasing number of human diseases including cancer. Autophagy inhibition accelerates the demise of tumor cells that are subjected to chemo-or radiotherapy, thereby constituting an interesting target for the development of anticancer strategies. However, several oncosuppressor proteins and oncoproteins have been recently shown to stimulate and inhibit the autophagic flow, respectively, suggesting that autophagy exerts bona fide tumor-suppressive functions. In this review, we will discuss the mechanisms by which autophagy may prevent oncogenesis.

Original languageEnglish
Pages (from-to)2251-2269
Number of pages19
JournalAntioxidants and Redox Signaling
Issue number11
Publication statusPublished - Jun 1 2011

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Physiology
  • Clinical Biochemistry


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