title: Structural insights into the function of human caveolin 1.
abstract: Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this paper, we used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported.
authors.affiliation: Department of Experimental Biology, University of Bologna, Via Selmi 3, 40126 Bologna, Italy. enzo.spisni@unibo.it
authors.forename: Enzo
authors.initials: E
authors.lastname: Spisni
authors.forename: Vittorio
authors.initials: V
authors.lastname: Tomasi
authors.forename: Alessandro
authors.initials: A
authors.lastname: Cestaro
authors.forename: Silvio C E
authors.initials: SC
authors.lastname: Tosatto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D051242:Caveolin 1 / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D019295:Computational Biology; D006801:Humans; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D051242:Caveolin 1