A curated resource to study the brain RNA expression patterns of the genes that regulate palmitoylation is presented, alongside a detailed exploration of how these patterns can inform future research.

Recruitment of NLRP3 to the Golgi is controlled by the reversible addition of a lipid anchor adjacent to the polybasic region.

ZDHHC14 controls palmitoylation and axon initial segment targeting of PSD93 and Kv1-family potassium channels, events that are essential for normal neuronal excitability.

Cycles of palmitoylation-depalmitoylation by an upstream palmitoyltransferase allow precise tuning of DHHC6 activity, which in turn regulates the abundance and function of key ER proteins involved in protein folding, degradation, ER architecture and calcium homeostasis.

Posttranslational protein palmitoylation and palmitoyl acyltransferase-substrate specificity emerge as a novel mechanism specifying the functional identity of neuronal substrates during the development of the central nervous system.

ORAI1 ion channel lipid modification is required for a proper immune synapse formation and T cell activation.

A systemic proteome of the pellicle organelle inner membrane complex (IMC) provides new insight for the intraerythrocytic proliferation of malaria parasite and identifies the palmitoyl-acyl-transferase DHHC2 as a key enzyme regulating the localization of IMC proteins through palmitoylation.

The two H2A.Z isoforms have specific interactors which mediate their differential effects on gene expression.

This article reviews the latest studies that have used super-resolution microscopy and cluster analysis methodologies to study the mechanism of protein kinase signalling hubs and their organisation at nanoscale.