Sean Munro

This study identifies TMEM115 as a two-factor component with Rab6A that recruits the golgin TMF1 to the Golgi apparatus, with implications for protein trafficking and disease.

The paper shows that p115 binds directly to Sec16A, a protein that organizes ER exit sites, and this interaction affects secretion efficiency.

This study determines the structure of the COPI vesicle coat with GOLPH3 and shows how it preferentially binds Golgi residents at late cisternae through coincidence detection of COPI and lipid.

This study identifies RABGAP1 as a sensor that modulates APP trafficking and processing by regulating RAB activity on endosomal subdomains, with implications for Alzheimer's disease.

The paper tracks exocytic vesicle movements in epithelial cells to show microtubule organisation controls apical secretion and reveals spatially organised ECM secretion.

This study identifies FAM114A proteins as adaptors that bind Golgi enzymes and contribute to COPI vesicle recycling specificity in the Golgi stack.

This study systematically identifies structure-specific protein-protein interactions using LiP-MS, demonstrating its application to alpha-synuclein in Parkinson's disease.

The paper identifies a mechanism by which TBC1D23 recognizes transport vesicles destined for the Golgi through direct binding to a shared cargo motif.

The paper develops an 'Unknome database' to prioritize understudied proteins and validates their functions using Drosophila RNAi and CRISPR/Cas9.