Structural insights into the function of human caveolin 1.

Enzo Spisni; Vittorio Tomasi; Alessandro Cestaro; Silvio C E Tosatto

doi:10.1016/j.bbrc.2005.10.099

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Structural insights into the function of human caveolin 1.

Enzo Spisni·Vittorio Tomasi·Alessandro Cestaro·Silvio C E Tosatto

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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.

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Amino Acid Sequence Animals Caveolin 1 Cell Membrane Computational Biology Humans Molecular Sequence Data Sequence Alignment Sequence Homology, Amino Acid Journal Article Research Support, Non-U.S. Gov't

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Enzo Spisni, Vittorio Tomasi, Alessandro Cestaro, Silvio C E Tosatto. 2005-10-26. Structural insights into the function of human caveolin 1.. https://doi.org/10.1016/j.bbrc.2005.10.099

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