The different roles of selective autophagic protein degradation in mammalian cells

Wang, Dawei; Peng, Zhen-ju; Ren, Guang-fang; Wang, Guangxin

doi:10.18632/oncotarget.5776

Cited by 47 publications

(45 citation statements)

References 190 publications

(127 reference statements)

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“…Under the stimulation of harmful factors in the internal and external environments, autophagy is activated in response to the stress of the cell. It renews the organelle and carries out cell metabolism, maintains cellular homeostasis, and plays an important role in the development, differentiation, and senescence [ 20 , 21 , 22 , 23 , 24 , 25 ].…”

Section: Neuronal Death In Nddsmentioning

confidence: 99%

Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases

Luo

Sandhu

Rungratanawanich

et al. 2020

IJMS

105

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With aging, the nervous system gradually undergoes degeneration. Increased oxidative stress, endoplasmic reticulum stress, mitochondrial dysfunction, and cell death are considered to be common pathophysiological mechanisms of various neurodegenerative diseases (NDDs) such as Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), organophosphate-induced delayed neuropathy (OPIDN), and amyotrophic lateral sclerosis (ALS). Autophagy is a cellular basic metabolic process that degrades the aggregated or misfolded proteins and abnormal organelles in cells. The abnormal regulation of neuronal autophagy is accompanied by the accumulation and deposition of irregular proteins, leading to changes in neuron homeostasis and neurodegeneration. Autophagy exhibits both a protective mechanism and a damage pathway related to programmed cell death. Because of its “double-edged sword”, autophagy plays an important role in neurological damage and NDDs including AD, PD, HD, OPIDN, and ALS. Melatonin is a neuroendocrine hormone mainly synthesized in the pineal gland and exhibits a wide range of biological functions, such as sleep control, regulating circadian rhythm, immune enhancement, metabolism regulation, antioxidant, anti-aging, and anti-tumor effects. It can prevent cell death, reduce inflammation, block calcium channels, etc. In this review, we briefly discuss the neuroprotective role of melatonin against various NDDs via regulating autophagy, which could be a new field for future translational research and clinical studies to discover preventive or therapeutic agents for many NDDs.

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Section: Neuronal Death In Nddsmentioning

confidence: 99%

Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases

Luo

Sandhu

Rungratanawanich

et al. 2020

IJMS

105

View full text Add to dashboard Cite

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“…CMA of soluble proteins has been most commonly studied. But type III CD38 is not the only membrane protein degraded through CMA (63). Others include the ryanodine receptor (62), a calcium channel in the ER targeted by cADPR, and the epidermal growth factor receptor (64).…”

Section: Regulation Of Type III Cd38mentioning

confidence: 99%

Resolving the topological enigma in Ca2+ signaling by cyclic ADP-ribose and NAADP

Lee

Zhao

2019

Journal of Biological Chemistry

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Edited by Mike Shipston Cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) are two structurally distinct messengers that mobilize the endoplasmic and endolysosomal Ca 2؉ stores, respectively. Both are synthesized by the CD38 molecule (CD38), which has long been thought to be a type II membrane protein whose catalytic domain, intriguingly, faces to the outside of the cell. Accordingly, for more than 20 years, it has remained unresolved how CD38 can use cytosolic substrates such as NAD and NADP to produce messengers that target intracellular Ca 2؉ stores. The discovery of type III CD38, whose catalytic domain faces the cytosol, has now begun to clarify this topological conundrum. This article reviews the ideas and clues leading to the discovery of the type III CD38; highlights an innovative approach for uncovering its natural existence; and discusses the regulators of its activity, folding, and degradation. We also review the compartmentalization of cADPR and NAADP biogenesis. We further discuss the possible mechanisms that promote type III CD38 expression and appraise a proposal of a Ca 2؉-signaling mechanism based on substrate limitation and product translocation. The surprising finding of another enzyme that produces cADPR and NAADP, sterile ␣ and TIR motif-containing 1 (SARM1), is described. SARM1 regulates axonal degeneration and has no sequence similarity with CD38 but can catalyze the same set of multireactions and has the same cytosolic orientation as the type III CD38. The intriguing finding that SARM1 is activated by nicotinamide mononucleotide to produce cADPR and NAADP suggests that it may function as a regulated Ca 2؉-signaling enzyme like CD38.

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“…ATG8 family contains two subfamilies that contain at least seven proteins in humans. The MAP1LC3 or LC3 group includes MAP1LC3A, MAP1LC3B, and MAP1LC3C, and the γ-aminobutyric acid type A receptor-associated protein (GABARAP) group includes GABARAP, GABARAP-like1 (GABARAPL1), GABARAPL2 and GABARAPL3 (Kalvari et al 2014;Wang et al 2015). Another protein, p62/SQSTM1, a polyubiquitin-binding protein interacts with LC3-II and both get degraded at the lysosomes (Pankiv et al 2007).…”

Section: Autophagic Degradation and Escrtsmentioning

confidence: 99%

ESCRTs and associated proteins in lysosomal fusion with endosomes and autophagosomes

Majumder

Chakrabarti

2016

Biochem. Cell Biol.

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Endolysosomal and autophagosomal degradation pathways are highly connected at various levels, sharing multiple molecular effectors that modulate them individually or simultaneously. These two lysosomal degradative pathways are primarily involved in the disposal of cargo internalized from the cell surface or long-lived proteins or aggregates and aged organelles present in the cytosol. Both of these pathways involve a number of carefully regulated vesicular fusion events that are dependent on ESCRT proteins. The ESCRT proteins especially ESCRT-I and III participate in the regulation of fusion events between autophagosome/amphisome and lysosome. Along with these, a number of functionally diverse ESCRT associated and regulatory proteins such as, endosomal PtdIns (3) P 5-kinase Fab1, ALIX, mahogunin ring finger 1, atrogin 1, syntaxin 17, ATG12-ATG3 complex, and protein kinase CK2α are involved in fusion events in either or both the lysosomal degradative pathways.

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The different roles of selective autophagic protein degradation in mammalian cells

Cited by 47 publications

References 190 publications

Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases

Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases

Resolving the topological enigma in Ca2+ signaling by cyclic ADP-ribose and NAADP

ESCRTs and associated proteins in lysosomal fusion with endosomes and autophagosomes

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