A novel role for a glycolytic pathway kinase in regulating autophagy has implications in cancer therapy. Issue 7 (3rd July 2017)

• Record Type: Journal Article
• Authors: Ariosa, Aileen R.; Klionsky, Daniel J.
• Is Part Of: Autophagy. Volume 13:Issue 7(2017)
• Page Start: 1091
• Page End: 1092
• Publication Date: 2017-07-03
• Subjects: autophagy -- BECN1 -- cancer -- glutamine -- PGK1 -- stress; Autophagic vacuoles -- Periodicals; Apoptosis -- Periodicals; Cell death -- Periodicals; Lysosomes -- Periodicals; Degeneration (Pathology) -- Periodicals; Autophagy -- Periodicals; Cell Death -- Periodicals; Lysosomes -- Periodicals; Periodicals; 571.936
• DOI: 10.1080/15548627.2017.1321723
• Languages: English
• ISSNs: 1554-8627

Abstract

ABSTRACT: When it comes to cancer initiation and progression, macroautophagy/autophagy seemingly acts in a contradictory fashion, serving either as a suppressive factor that functions to protect against tumor formation or as a support mechanism that sustains the disease itself through its cytoprotective functions. In tumor suppression, autophagy assists by restricting oxidative stress and curbing genomic instability that could possibly cause oncogenic mutations. However, in certain circumstances, autophagy can also promote cancer by providing nourishment and by limiting stress-response pathways, leading to cancer cell survival and rapid proliferation. Thus, autophagy's role in oncogenesis is highly context-dependent and varies from one cancer type to another. As a consequence, identifying the mechanisms that alter and rewire autophagic regulation and flux is extremely crucial to target autophagy as a possible avenue for anticancer treatment. In a recent study, Qian et al. endeavored to identify one such key regulatory pathway in hypoxia- and glutamine deprivation-induced autophagy in tumorigenic cells. In this pathway, phosphatidylinositol 3-phosphate (PtdIns3P) production by the class III phosphatidylinositol 3-kinase (PtdIns3K) complex is greatly improved through a cascade of posttranslational modifications that culminates in the phosphorylation of the scaffolding protein BECN1 by the glycolytic pathway kinase PGK1.