Rab8
- S-acylation regulates the trafficking and stability of the unconventional Q-SNARE STX19
Highlighted Article: The Q-SNARE STX19 is S-acylated by Golgi-localised S-acyltransferases, and this lipidation targets the protein to MICAL-L1-positive tubular recycling endosomes and also protects it from proteasomal degradation.
- Endocytic turnover of Rab8 controls cell polarization
Highlighted Article: GRAF1 mediates inactivation and endocytic removal of Rab8 from cell surface protrusions, thereby facilitating dynamic adjustment of the polarity axis.
- A ternary complex comprising transportin1, Rab8 and the ciliary targeting signal directs proteins to ciliary membranes
Summary: Transportin1 and Rab8 can simultaneously bind to the ciliary targeting signal in a guanine-nucleotide-dependent manner. The resulting ternary complex can target a membrane protein to cilia.
- A novel high-content analysis tool reveals Rab8-driven cytoskeletal reorganization through Rho GTPases, calpain and MT1-MMP
Summary: Rab8 can induce Rac1- and Tiam1-dependent cortical actin polymerization and focal adhesion disassembly through the proteases MT1-MMP and calpain, and Rho-GTPase-dependent mechanisms.
- The small GTPase Rab8 interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse
Highlighted Article: The ciliary regulator Rab8 is co-opted by T-cells during the assembly of the immune synapse to promote the VAMP-3-dependent step of polarized T-cell receptor recycling.