Palmitoylation of the Alternative Amino Terminus of the BTK-C Isoform Controls Subcellular Distribution and Signaling.

ABSTRACT:

Background

The alternative transcriptional isoform of Bruton's tyrosine kinase, BTK-C, is expressed in a wide variety of epithelial tumor types where it impacts apoptosis resistance, therapeutic escape, and glucose uptake. The initial exon in BTK-C encodes a 34 amino acid extension of the amino terminus of the canonical BTK-A isoform. Its function is unknown.

Materials and methods

Site-directed mutagenesis, acylation assays and expression studies in cancer cell lines were used to determine the effects that the BTK-C first exon sequence has on kinase activity, subcellular localization and cell physiology. Analysis of BTK-C expression in tumors was conducted using genomic databases.

Results

BTK-C is palmitoylated on two cysteine residues. BTK-C localization at the plasm

SUBMITTER: Kokabee M 

PROVIDER: S-EPMC9247882 | biostudies-literature | 2022 Jul-Aug

REPOSITORIES: biostudies-literature