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Biochem Biophys Res Commun. 2005 Dec 23;338(3):1383-90. Epub 2005 Oct 26.

Structural insights into the function of human caveolin 1.

Author information

1
Department of Experimental Biology, University of Bologna, Via Selmi 3, 40126 Bologna, Italy. enzo.spisni@unibo.it

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.

PMID:
16263077
DOI:
10.1016/j.bbrc.2005.10.099
[Indexed for MEDLINE]

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