In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases
Open Biology, 2022 Protein S-acylation, more commonly known as protein palmitoylation, is a biological process defined by the covalent attachment of long chain fatty acids onto cysteine residues of a protein, effectively altering the local hydrophobicity and influencing its stability, localization and overall function.
R. Elliot Murphy, Anirban Banerjee
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The C-terminal domain of zDHHC2 contains distinct sorting signals that regulate intracellular localisation in neurons and neuroendocrine cells [PDF]
, 2017 The S-acyltransferase zDHHC2 mediates dynamic S-acylation of PSD95 and AKAP79/150, which impacts synaptic targeting of AMPA receptors. zDHHC2 is responsive to synaptic activity and catalyses the increased S-acylation of PSD95 that occurs following action
Bushell, Trevor J. +4 more
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Editorial: role of protein palmitoylation in synaptic plasticity and neuronal differentiation [PDF]
, 2020 © The Author(s), 2020. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Yoshii, A., & Green, W. N.
Green, William N., Yoshii, Akira
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Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualisation, identification and quantification of N-myristoylation, N- and S-acylation, Ocholesterylation, S-farnesylation and S-geranylgeranylation [PDF]
, 2021 Protein lipidation is one of the most widespread post-translational modifications (PTMs) found in nature, regulating protein function, structure and subcellular localization.
Ciepla, Paulina +6 more
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The GolgiS-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity andS-acylation activity [PDF]
Molecular Biology of the Cell, 2014 S-acylation, the attachment of fatty acids onto cysteine residues, regulates protein trafficking and function and is mediated by a family of zDHHC enzymes. The S-acylation of peripheral membrane proteins has been proposed to occur at the Golgi, catalyzed by an S-acylation machinery that displays little substrate specificity. To advance understanding of
Lemonidis, Kimon +4 more
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A palmitoyl transferase chemical genetic system to map ZDHHC-specificS-acylation
, 2023 AbstractThe 23 human ZDHHCS-acyltransferases catalyze long-chainS-acylation at cysteine residues across an extensive network of hundreds of proteins important for normal physiology or dysregulated in disease. Here we present a technology platform to directly map the protein substrates of a specific ZDHHC for the first time at the whole proteome level ...
Ocasio CA +13 more
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Disruption of the Zdhhc9 intellectual disability gene leads to behavioural abnormalities in a mouse [PDF]
, 2018 Protein S-acylation is a widespread post-translational modification that regulates the trafficking and function of a diverse array of proteins. This modification is catalysed by a family of twenty-three zDHHC enzymes that exhibit both specific and ...
Brett, Ros R. +6 more
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A palmitoyl transferase chemical genetic system to map ZDHHC-specific S-acylation [PDF]
, 2023 The 23 human ZDHHC S-acyltransferases catalyze long-chain S-acylation at cysteine residues across an extensive network of hundreds of proteins important for normal physiology or dysregulated in disease.
Baggelaar, Marc +13 more
core
Site specific deacylation by ABHD17a controls BK channel splice variant activity [PDF]
, 2020 S-Acylation, the reversible post-translational lipid modification of proteins, is an important mechanism to control the properties and function of ion channels and other polytopic transmembrane proteins.
McClafferty, Heather +2 more
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The Intrinsically Disordered Termini of zDHHC S-Palmitoyltransferases Facilitate Multiple Regulatory Functions [PDF]
Biophysical Journal, 2015 zDHHC protein acyltransferases (PATs) are a family of membrane proteins that catalyze the reversible post-translational lipidation known as palmitoylation, a process essential to normal cellular function through facilitation of membrane attachment, subcellular trafficking, and protein stability.
Krishna D., Reddy +5 more
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