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First published online July 25, 2006
doi: 10.1242/10.1242/jcs.03072
Commentary |
Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309-0347, USA
e-mail: odorizzi{at}colorado.edu
Accepted 1 June 2006
Alix is a cytosolic protein in mammalian cells that was originally identified on the basis of its association with pro-apoptotic signaling. More recent evidence has established that Alix has a hand in regulating other cellular mechanisms, including endocytic membrane trafficking and cell adhesion. Although Alix appears to participate directly in these various activities, the role it plays in each process has largely been inferred from the functions of proteins with which it interacts. For example, recruitment of Alix to endosomes is mediated by its N-terminal Bro1 domain, the structure of which was recently solved for its yeast orthologue, Bro1. The diversity of Alix functions is due to its proline-rich C-terminus, which provides multiple protein-binding sites. With this blueprint in hand, we can now ask whether Alix acts simply as an adaptor that links different proteins into networks or, instead, contributes a specific function to distinct molecular machineries.
Key words: Alix, Bro1, MVB, Endocytosis, Apoptosis
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