Abstract
The golgin family gives identity and structure to the Golgi apparatus and is part of a complex protein network at the Golgi membrane. The golgin p115 is targeted by the GTPase Rab1a, contains a large globular head region and a long region of coiled-coil which forms an extended rod-like structure. p115 serves as vesicle tethering factor and plays an important role at different steps of vesicular transport. Here we present the 2.2 Å-resolution X-ray structure of the globular head region of p115. The structure exhibits an armadillo fold that is decorated by elongated loops and carries a C-terminal non-canonical repeat. This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.
Highlights
Membrane trafficking in eukaryotic cells is an example for the modular organization of cellular activity
Interaction of Rab1a and p115 is thought to tether coat-protein complex II (COP II) vesicles to each other, promoting homotypic vesicle fusion [3]
The C-terminal region of p115 binds to GM130 and giantin, two further coiled-coil tethers localized at the Golgi membrane [4]
Summary
Membrane trafficking in eukaryotic cells is an example for the modular organization of cellular activity. They can be divided into multi-subunit tethering complexes and proteins containing an extended coiled-coil region. We used a construct comprising the globular head region of p115 (p115GHR, residues Asp54 to Tyr629) for crystallization (Fig. 1).
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
