Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy

摘要: Highly stable oligomeric complexes of the monotopic membrane protein caveolin serve as fundamental building blocks caveolae. Current evidence suggests these are disc shaped, but details their structural organization and how they assemble poorly understood. Here, we address questions using single particle electron microscopy negatively stained recombinant 8S human Caveolin-1. We show that toroidal structures ~15 nm in diameter consist an outer ring, inner central protruding stalk. Moreover, map position N- C-termini determine role complex assembly, visualize heterologous Our findings provide critical insights into features allow us to propose a new model for highly membrane-embedded generated.