Trs20 is required for TRAPP II assembly.

ABSTRACT: The modular TRAPP complexes act as nucleotide exchangers to activate the Golgi Ypt/Rab GTPases, Ypt1 and Ypt31/Ypt32. In yeast, TRAPP I acts at the cis-Golgi and its assembly and structure are well characterized. In contrast, TRAPP II acts at the trans-Golgi and is poorly understood. Especially puzzling is the role of Trs20, an essential TRAPP I/II subunit required neither for the assembly of TRAPP I nor for its Ypt1-exchange activity. Mutations in Sedlin, the human functional ortholog of Trs20, cause the cartilage-specific disorder SEDT. Here we show that Trs20 interacts with the TRAPP II-specific subunit Trs120. Furthermore, the Trs20-Trs120 interaction is required for assembly of TRAPP II and for its Ypt32-exchange activity. Finally, Trs20-D46Y, with a single-residue substitution equiva

SUBMITTER: Taussig D 

PROVIDER: S-EPMC3660434 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature