Structural Characterization for N-Terminal Domain of Caveolin-1

Abstract

Caveolin-1 is a principal protein in the plasma membrane microdomains called caveolae. Caveolae play an important role in the transcytosis and pinocytosis. Therefore, caveolin-1 is most likely to work for the membrane dynamic events. In addition, caveolin-1 interacts with various signaling molecules. Although caveolin-1 possesses a variety of physiological functions, its structural properties were little construed. Here we analyzed the structural dynamics of the N-terminal caveolin-1 (residues 1-101), in order to better understand the structural properties in terms of its versatile functionality. We first analyzed its oligomeric form using GST-fused N-terminal domain, revealing that it equilibrates between a dimer and monomers in a concentration-dependent manner. The N-terminal domain of caveolin-1 was previously found to form a heptamer, so that our data suggest the dimeric form as an intermediate structure for the heptamer formation. Then, we obtained the folding profile, which indicated that GH2O is about 0.5 ± 0.03 kcal / mol. The stability of N-terminal domain is relatively low, indicating that N-terminal domain may not be crystalline. Conclusively, the dynamic and flexible structure of N-terminal domain appears more favorable to maintain the versatile functions of caveolin-1.