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ULK/Atg1: phasing in and out of autophagy.
Wang, Bo; Pareek, Gautam; Kundu, Mondira.
Afiliação
  • Wang B; State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen 361102, China; Shenzhen Research Institute of Xiamen University, Shenzhen, 518057, China.
  • Pareek G; Department of Cell and Molecular Biology, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
  • Kundu M; Department of Cell and Molecular Biology, St Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: Mondira.Kundu@STJUDE.ORG.
Trends Biochem Sci ; 49(6): 494-505, 2024 Jun.
Article em En | MEDLINE | ID: mdl-38565496
ABSTRACT
Autophagy - a highly regulated intracellular degradation process - is pivotal in maintaining cellular homeostasis. Liquid-liquid phase separation (LLPS) is a fundamental mechanism regulating the formation and function of membrane-less compartments. Recent research has unveiled connections between LLPS and autophagy, suggesting that phase separation events may orchestrate the spatiotemporal organization of autophagic machinery and cargo sequestration. The Unc-51-like kinase (ULK)/autophagy-related 1 (Atg1) family of proteins is best known for its regulatory role in initiating autophagy, but there is growing evidence that the functional spectrum of ULK/Atg1 extends beyond autophagy regulation. In this review, we explore the spatial and temporal regulation of the ULK/Atg1 family of kinases, focusing on their recruitment to LLPS-driven compartments, and highlighting their multifaceted functions beyond their traditional role.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Autofagia / Proteína Homóloga à Proteína-1 Relacionada à Autofagia Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Autofagia / Proteína Homóloga à Proteína-1 Relacionada à Autofagia Idioma: En Ano de publicação: 2024 Tipo de documento: Article