Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine
palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic …

RAS proteins require membrane association for their biologic activity, making this
association a logical target for anti-RAS therapeutics. Lipid modification of RAS proteins by a …

Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is
emerging as a ubiquitous mechanism to control the properties and function of a diverse …

Long, short and medium chain fatty acids are covalently attached to hundreds of proteins.
Each fatty acid confers distinct biochemical properties, enabling fatty acylation to regulate …

Dynamic changes in protein S-palmitoylation are critical for regulating protein localization
and signaling. Only two enzymes-the acyl-protein thioesterases APT1 and APT2–are known …

Multiple Ras proteins, including N-Ras, depend on a palmitoylation/depalmitoylation cycle to
regulate their subcellular trafficking and oncogenicity. General lipase inhibitors such as …

Protein depalmitoylation describes the removal of thioester-linked long chain fatty acids from
cysteine residues in proteins. For many S-palmitoylated proteins, this process is promoted …

Huntington disease (HD) damages the corticostriatal circuitry in large part by impairing
transport of brain-derived neurotrophic factor (BDNF). We hypothesized that improving …

Protein palmitoylation, in which C16 fatty acid chains are attached to cysteine residues via a
reversible thioester linkage, is one of the most common lipid modifications and plays …

S-Acylation (commonly referred to as S-palmitoylation) is a post-translational modification
consisting in the covalent attachment of an acyl chain to a cysteine residue of the target …