<scp>DHHC5</scp> facilitates oligodendrocyte development by palmitoylating and activating <scp>STAT3</scp>

Ma, Yanchen; Liu, Huiqing; Ou, Zhimin; Chen, Qi; Xing, Rui; Wang, Shiyun; Han, Yinuo; Zhao, Tong‐Jin; Chen, Ying

doi:10.1002/glia.24113

Cited by 11 publications

(6 citation statements)

References 53 publications

(56 reference statements)

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“…S- palmitoylation is defined as the reversible formation of a cysteine residue thioester bond with the fatty acid palmitate, and is the most prevalent post-translational lipid modification in the brain. Dynamic changes in S -palmitoylation are critical for neuronal development and synaptic plasticity ( Fukata et al, 2013 ; Fukata and Fukata, 2010 ; Globa and Bamji, 2017 ; Matt et al, 2019 ), oligodendrocyte differentiation and myelination ( Ma et al, 2022 ; Schneider et al, 2005 ), and astrocyte proliferation ( Yuan et al, 2021 ). Furthermore, numerous neurological and psychiatric diseases have now been attributed to mutations in the genes encoding palmitoylating and de-palmitoylating enzymes, including schizophrenia, intellectual disability and CLN1 disease ( Mukai et al, 2004 ; Nita et al, 2016 ; Raymond et al, 2007 ), underscoring the importance of proper regulation of S -palmitoylation for normal brain function.…”

Section: Introductionmentioning

confidence: 99%

Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq

Wild

Hogg

Flibotte

et al. 2022

eLife

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Protein S-palmitoylation is a reversible post-translational lipid modification that plays a critical role in neuronal development and plasticity, while dysregulated S-palmitoylation underlies a number of severe neurological disorders. Dynamic S-palmitoylation is regulated by a large family of ZDHHC palmitoylating enzymes, their accessory proteins, and a small number of known de-palmitoylating enzymes. Here, we curated and analyzed expression data for the proteins that regulate S-palmitoylation from publicly available RNAseq datasets, providing a comprehensive overview of their distribution in the mouse nervous system. We developed a web-tool that enables interactive visualization of the expression patterns for these proteins in the nervous system (http://brainpalmseq.med.ubc.ca/), and explored this resource to find region and cell-type specific expression patterns that give insight into the function of palmitoylating and de-palmitoylating enzymes in the brain and neurological disorders. We found coordinated expression of ZDHHC enzymes with their accessory proteins, de-palmitoylating enzymes and other brain-expressed genes that included an enrichment of S-palmitoylation substrates. Finally, we utilized ZDHHC expression patterns to predict and validate palmitoylating enzyme-substrate interactions.

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Section: Introductionmentioning

confidence: 99%

Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq

Wild

Hogg

Flibotte

et al. 2022

eLife

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“…ZDHHC-mediated palmitoylation is a post-translational regulator of protein intracellular trafficking, subcellular localization, stability and activity as well as protein-protein interactions, and has been shown to regulate differentiation of multiple cell types [ 21 , [26] , [27] , [28] , [29] ]. However, it is unclear whether palmitoylation is involved in osteoclast differentiation and which ZDHHC is the key palmitoylation enzyme involved in this process.…”

Section: Discussionmentioning

confidence: 99%

Pharmacological inhibition of protein S-palmitoylation suppresses osteoclastogenesis and ameliorates ovariectomy-induced bone loss

Zhang

Liao

et al. 2023

Journal of Orthopaedic Translation

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“…We speculate that the palmitoyl acyltransferases for target proteins might be cell‐ or tissue‐specific. For instance, zDHHC5 was shown to facilitate STAT3 palmitoylation in oligodendrocytes (Ma et al , 2022), while only overexpression of zDHHC7 and zDHHC3 could increase the palmitoylation level of STAT3 in HEK293T cells (Zhang et al , 2020).…”

Section: Discussionmentioning

confidence: 99%

KLF10 promotes nonalcoholic steatohepatitis progression through transcriptional activation of zDHHC7

et al. 2022

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Nonalcoholic steatohepatitis (NASH), characterized by hepatic steatosis, inflammation, and liver injury, has become a leading cause of end‐stage liver diseases and liver transplantation. Krüppel‐like factors 10 (KLF10) is a Cys2/His2 zinc finger transcription factor that regulates cell growth, apoptosis, and differentiation. However, whether it plays a role in the development and progression of NASH remains poorly understood. In the present study, we found that KLF10 expression was selectively upregulated in the mouse models and human patients with NASH, compared with simple steatosis (NAFL). Gain‐ and loss‐of function studies demonstrated that hepatocyte‐specific overexpression of KLF10 aggravated, whereas its depletion alleviated diet‐induced NASH pathogenesis in mice. Mechanistically, transcriptomic analysis and subsequent functional experiments showed that KLF10 promotes hepatic lipid accumulation and inflammation through the palmitoylation and plasma membrane localization of fatty acid translocase CD36 via transcriptionally activation of zDHHC7. Indeed, both expression of zDHHC7 and palmitoylation of CD36 are required for the pathogenic roles of KLF10 in NASH development. Thus, our results identify an important role for KLF10 in NAFL‐to‐NASH progression through zDHHC7‐mediated CD36 palmitoylation.

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DHHC5 facilitates oligodendrocyte development by palmitoylating and activating STAT3

Cited by 11 publications

References 53 publications

Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq

Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq

Pharmacological inhibition of protein S-palmitoylation suppresses osteoclastogenesis and ameliorates ovariectomy-induced bone loss

KLF10 promotes nonalcoholic steatohepatitis progression through transcriptional activation of zDHHC7

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