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.

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.

The protein-lipid modification palmitoylation targets the kinase LIMK1 to dendritic spines to ensure precise control of the size of individual spines in response to synaptic activation.

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.

Mitochondria can trigger massive endocytosis by releasing coenzyme A into the cytoplasm and thereby promoting the addition of fatty acids to surface membrane proteins.

NMDA receptor function is regulated by protein depalmitoylation during visual cortical maturation and is dysfunctional in infantile neuronal ceroid lipofuscinosis.

Palmitate turnover is controlled by distinct enzyme families with different specificities.

A new insight into the role of syntaxin1's juxtamembrane region in controlling palmitoylation and spontaneous neurotransmitter release.

A step of contact establishment preceding stable membrane attachment by palmitoylation is identified.