Results 31 to 40 of about 473 (132)
Dysfunctional Decidual CD4<sup>+</sup>T Cells Induce Recurrent Pregnancy Loss via Palmitoylation-Dependent Tim-3 Lysosomal Sorting and Degradation. [PDF]
Adv Sci (Weinh)Dysfunctional decidual CD4+T cells induce recurrent pregnancy loss via palmitoylation‐dependent Tim‐3 lysosomal sorting and degradation. The integrated bioinformatics, proteomic, functional and model studies elucidate that Tim‐3 is palmitoylated by ZDHHC3 at Cys9. Sortilin bound to and directed palmitoylated Tim‐3 toward lysosome degradation, resulting
Cui L +6 more
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The zDHHC family of S-acyltransferases [PDF]
Biochemical Society Transactions, 2015 The discovery of the zDHHC family of S-acyltransferase enzymes has been one of the major breakthroughs in the S-acylation field. Now, more than a decade since their discovery, major questions centre on profiling the substrates of individual zDHHC enzymes (there are 24 ZDHHC genes and several hundred S-acylated proteins), defining the mechanisms of ...
Kimon Lemonidis +7 more
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Frontiers in Physiology, 2014 Mechanisms that control surface expression and/or activity of large conductance calcium-activated potassium (BK) channels are important determinants of their (patho)physiological function.
Michael J Shipston, Shipston Michael J
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Regulatory effects of post-translational modifications on zDHHC S-acyltransferases [PDF]
Journal of Biological Chemistry, 2020 The human zDHHC S-acyltransferase family comprises 23 enzymes that mediate the S-acylation of a multitude of cellular proteins, including channels, receptors, transporters, signaling molecules, scaffolds, and chaperones. This reversible post-transitional modification (PTM) involves the attachment of a fatty acyl chain, usually derived from palmitoyl ...
Filip Zmuda, Luke Chamberlain
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Substrate selectivity in the zDHHC family of S-acyltransferases [PDF]
Biochemical Society Transactions, 2017 S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound ‘zDHHC’ enzymes. S-acylation predominantly results in anchoring of soluble proteins to membrane compartments or in the trafficking of membrane proteins to different compartments.
Kimon Lemonidis +5 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 +4 more
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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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Targeted degradation of zDHHC-PATs decreases substrate S-palmitoylation
PLOS ONEReversible S-palmitoylation of protein cysteines, catalysed by a family of integral membrane zDHHC-motif containing palmitoyl acyl transferases (zDHHC-PATs), controls the localisation, activity, and interactions of numerous integral and peripheral membrane proteins.
Mingjie Bai +11 more
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Control of protein palmitoylation by regulating substrate recruitment to a zDHHC-protein acyltransferase [PDF]
Communications Biology, 2020 AbstractAlthough palmitoylation regulates numerous cellular processes, as yet efforts to manipulate this post-translational modification for therapeutic gain have proved unsuccessful. The Na-pump accessory sub-unit phospholemman (PLM) is palmitoylated by zDHHC5.
Fiona Plain +6 more
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Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases
Current Opinion in Structural Biology, 2022 S-acylation is a reversible posttranslational modification, where a long-chain fatty acid is attached to a protein through a thioester linkage. Being the most abundant form of lipidation in humans, a family of twenty-three human zDHHC integral membrane enzymes catalyze this reaction. Previous structures of the apo and lipid bound zDHHCs shed light into
Robbins Puthenveetil +2 more
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