The chaperone SmgGDS-607 has a dual role, both activating and inhibiting farnesylation of small GTPases.

ABSTRACT: Ras family small GTPases undergo prenylation (such as farnesylation) for proper localization to the plasma membrane, where they can initiate oncogenic signaling pathways. Small GTP-binding protein GDP-dissociation stimulator (SmgGDS) proteins are chaperones that bind and traffic small GTPases, although their exact cellular function is unknown. Initially, SmgGDS proteins were classified as guanine nucleotide exchange factors, but recent findings suggest that SmgGDS proteins also regulate prenylation of small GTPases in vivo in a substrate-selective manner. SmgGDS-607 recognizes the polybasic region and the CAAX box of several small GTPases and inhibits prenylation by impeding their entry into the geranylgeranylation pathway. Here, using recombinant and purified enzymes for pre

SUBMITTER: Garcia-Torres D 

PROVIDER: S-EPMC6682747 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature