The endoplasmic reticulum–localized enzyme zDHHC6 mediates S-acylation of short transmembrane constructs from multiple type I and II membrane proteins

Salaun, Christine; Tomkinson, Nicholas C.O.; Chamberlain, Luke H.

doi:10.1016/j.jbc.2023.105201

Cited by 5 publications

(1 citation statement)

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“…One still poorly understood step for most ZDHHC enzymes is how they recognize and bind their substrates. Four main factors have been proposed to provide specificity: (a) subcellular localization; (b) accessory proteins, which act as adaptors ( Salaun et al, 2020 ); (c) recognition between transmembrane regions ( Salaun et al, 2023 ); and (d) the presence of protein–protein interaction domains or motifs in the N-terminal and C-terminal domains of ZDHHCs. For example, ankyrin repeats are present in ZDHHC13 and 17, which mediate interaction with Huntington protein HTT ( Huang et al, 2009 ; Lemonidis et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications

Anwar,

van der Goot

2023

Journal of Cell Biology

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With a limited number of genes, cells achieve remarkable diversity. This is to a large extent achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid modifications that have the unique ability to confer hydrophobicity. The last decade has revealed that lipid modifications of proteins are extremely frequent and affect a great variety of cellular pathways and physiological processes. This is particularly true for S-acylation, the only reversible lipid modification. The enzymes involved in S-acylation and deacylation are only starting to be understood, and the list of proteins that undergo this modification is ever-increasing. We will describe the state of knowledge on the enzymes that regulate S-acylation, from their structure to their regulation, how S-acylation influences target proteins, and finally will offer a perspective on how alterations in the balance between S-acylation and deacylation may contribute to disease.

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