Williams TM , Lisanti MP .

T32-GM07288 NIGMS NIH HHS , T32 GM007288 NIGMS NIH HHS

Figure 1. A phylogenetic tree depicting the evolutionary relationships of all known caveolin protein sequences. Note that C. elegans Cav-2 was not included in this analysis because of its low similarity to the mammalian caveolins. GenBank-derived protein sequences were entered into the ClustalW program to generate a phylogenetic tree using the neighbor-joining method. Numbers indicate horizontal branch lengths, which correspond to the estimated evolutionary distances between the protein sequences.

Figure 2. Primary structure and topology of Cav-1. (a) The predicted membrane topology of Cav-1. Two caveolin-1 monomers are shown forming a dimer for simplicity, but about 14-16 monomers normally self-associate to form a single caveolin homo-oligomer (the caveolar assembly unit, akin to the clathrin triskelion). Note that both the amino- and carboxy-terminal domains are oriented towards the cytosolic face of the plasma membrane, with a hairpin loop structure inserted within the membrane bilayer. Modified from Razani et al. [42]. (b) The domains present in Cav-1. Note that the amino-terminal membrane-attachment domain is also called the caveolin scaffolding domain (CSD).

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