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Kocaturk NM, Gozuacik D. Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System. Front Cell Dev Biol. 2018;6:128doi: 10.3389/fcell.2018.00128.
Kocaturk, N. M., & Gozuacik, D. (2018). Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System. Frontiers in cell and developmental biology, 6128. https://doi.org/10.3389/fcell.2018.00128
Kocaturk, Nur Mehpare, and Gozuacik, Devrim. "Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System." Frontiers in cell and developmental biology vol. 6 (2018): 128. doi: https://doi.org/10.3389/fcell.2018.00128
Kocaturk NM, Gozuacik D. Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System. Front Cell Dev Biol. 2018 Oct 02;6:128. doi: 10.3389/fcell.2018.00128. eCollection 2018. PMID: 30333975; PMCID: PMC6175981.
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Front Cell Dev Biol. 2018 Oct 02;6:128. doi: 10.3389/fcell.2018.00128. eCollection 2018.

Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System.

Frontiers in cell and developmental biology

Nur Mehpare Kocaturk, Devrim Gozuacik

Affiliations

  1. Molecular Biology, Genetics and Bioengineering Program, Faculty of Engineering and Natural Sciences, Sabanci University, Istanbul, Turkey.
  2. Center of Excellence for Functional Surfaces and Interfaces for Nano Diagnostics (EFSUN), Sabanci University, Istanbul, Turkey.
  3. Nanotechnology Research and Application Center (SUNUM), Sabanci University, Istanbul, Turkey.

PMID: 30333975 PMCID: PMC6175981 DOI: 10.3389/fcell.2018.00128

Abstract

Autophagy and the ubiquitin-proteasome system (UPS) are the two major intracellular quality control and recycling mechanisms that are responsible for cellular homeostasis in eukaryotes. Ubiquitylation is utilized as a degradation signal by both systems, yet, different mechanisms are in play. The UPS is responsible for the degradation of short-lived proteins and soluble misfolded proteins whereas autophagy eliminates long-lived proteins, insoluble protein aggregates and even whole organelles (e.g., mitochondria, peroxisomes) and intracellular parasites (e.g., bacteria). Both the UPS and selective autophagy recognize their targets through their ubiquitin tags. In addition to an indirect connection between the two systems through ubiquitylated proteins, recent data indicate the presence of connections and reciprocal regulation mechanisms between these degradation pathways. In this review, we summarize these direct and indirect interactions and crosstalks between autophagy and the UPS, and their implications for cellular stress responses and homeostasis.

Keywords: UPS; autophagy; mitophagy; organelle homeostasis; proteasome; protein quality control; proteostasis; ubiquitylation

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