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

More and more in-depth studies have revealed that the occurrence and development of
tumors depend on gene mutation and tumor heterogeneity. The most important …

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 …

Enhanced sensitivity to Wnts is an emerging hallmark of a subset of cancers, defined in part
by mutations regulating the abundance of their receptors. Whether these mutations identify a …

Protein lipid modification involves the attachment of hydrophobic groups to proteins via
ester, thioester, amide, or thioether linkages. In this review, the specific click chemical …

Porcupine (PORCN) is a membrane bound O-acyltransferase that is required for Wnt
palmitoylation, secretion, and biologic activity. All evaluable human Wnts require PORCN for …

Expansion microscopy (ExM) allows super-resolution imaging on conventional fluorescence
microscopes, but has been limited to proteins and nucleic acids. Here we develop click-ExM …

The Hippo signaling pathway is responsible for regulating the function of TEAD family
transcription factors in metazoans. TEADs, with their co-activators YAP/TAZ, are critical for …

S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate)
onto cysteine residues via a labile thioester bond. This posttranslational modification …

Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is
converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein …