Rolf Jaussi

TL;DR: The findings define the molecular basis of CAP-Gly domain function, including the tubulin detyrosination-tyrosination cycle, and establish fundamental roles for the interaction between CAP-gly proteins and C-terminal EEY/F sequence motifs in regulating complex and dynamic cellular processes.

TL;DR: Structural analysis of a complex of tubulin and tubulin tyrosine ligase (TTL) reveals insights into TTL’s enzymatic mechanism, how it discriminates between α- and β-tubulin, and its possible evolutionary origin.

TL;DR: These findings provide a molecular basis for understanding the modular interaction modes between alpha-tubulin, CLIPs, EB proteins, and the dynactin-dynein motor complex and suggest that multiple low-affinity binding sites in different combinations control dynamic +TIP networks at microtubule ends.

TL;DR: The developed cloning strategy allows isolation of cDNAs encoding proteins for which a ligand is available and circumvents immobilisation of the libraries on solid-phase supports which hamper selective enrichment of clones expressing the desired protein.

TL;DR: The high-resolution crystal structure of the BoNT/A receptor-binding domain (BoNT/ a-RBD) in complex with the SV2C luminal domain (SV2C-LD) is determined, providing a strong platform for the development of novel antitoxin agents and for the rational design of Bo NT/A variants with improved therapeutic properties.