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Research progress on the role of TANK-binding kinase 1 in PINK1/Parkin- dependent and -independent mitophagy

DENG Hao¹, XIA Zhi^2,3, SHANG Hua-Yu^2,*

¹School of Sports Medicine and Health, Chengdu Sport University, Chengdu 610041, China；²College of Physical Education and Health, Wenzhou University, Wenzhou 325035, China；³Physical Education College of Jinggangshan University, Ji’an 343009, China

Abstract

Mitophagy is a process that selectively removes excess or damaged mitochondria and plays an important role in regulating intracellular mitochondrial mass and maintaining mitochondrial energy metabolism. TANK-binding kinase 1 (TBK1) is a multifunctional serine/threonine protein kinase, which is involved in the regulation of PTEN-induced putative kinase 1 (PINK1)/Parkin-dependent and -independent mitophagy. Recent studies have shown that TBK1 phosphorylates the autophagy related proteins, such as optineurin (OPTN), p62/sequestosome-1, Ras-related GTP binding protein 7 (Rab7), and mediates the binding of nuclear dot protein 52 (NDP52) to UNC-51 like autophagy activating kinase 1 (ULK1) complex, as well as the binding of TAX1-binding protein 1 (TAX1BP1) to microtubule-associated protein 1 light chain 3 (LC3), thereby enhancing PINK1/Parkin-dependent mitophagy. In addition, TBK1 is a direct substrate of AMP-activated protein kinase (AMPK)/ULK1 pathway, and its activation phosphorylates dynamin-related protein 1 (Drp1) and Rab7 to promote PINK1/Parkin-independent mitophagy. This article reviews the role and mechanism of TBK1 in regulating PINK1/Parkin-dependent and -independent mitophagy.

Key words: mitochondrion; mitophagy; TANK-binding kinase 1; PTEN-induced putative kinase 1; Parkin

Received: 　　Accepted:

Corresponding author: 尚画雨　　E-mail: santanasan@163.com

DOI: 10.13294/j.aps.2023.0061

Citing This Article：

DENG Hao, XIA Zhi, SHANG Hua-Yu. Research progress on the role of TANK-binding kinase 1 in PINK1/Parkin- dependent and -independent mitophagy. Acta Physiol Sin 2024; 76 (1): 161-172 (in Chinese with English abstract).