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Based upon the structure of the Bro1 domain in Bro1 , the Bro1 domains of Alix and Rim20 are predicted to span residues 1-366 and 1-387, respectively.

A Ribbon diagram of the Bro1 domain.

Other recent work, however, has implicated Alix in the control of MVB vesicle formation.

Since the late domains from different viruses are in some cases functionally interchangeable, there is clearly some level of redundancy.

Similarly, the proline-rich region of Bro1 is contained within a region required for interaction with Doa4.

Growth factor receptor endocytosis Alix appears to have a role in negative regulation of growth factor receptor endocytosis at the plasma membrane, which occurs upstream of ESCRT-mediated protein sorting at endosomes.

The wavy line connecting ESCRT-III to the membrane represents N-myristoylation of CHMP6, another subunit of ESCRT-III.

Two putative coiled-coil domains CC are located between residues 430-471 and residues 543-583 of Alix, whereas Bro1 and Rim20 are each predicted to have a single CC domain between residues 543-583 in Bro1 and 386-426 in Rim20.

B Phosphorylation of Alix by Src prevents Alix from binding SETA , thereby enabling association of Cbl with the SETA-endophilin complex as well as Cbl-mediated ubiquitylation, which promotes downregulation of receptors.

In this regard, it is interesting that Alix is abundant within extracellular vesicles known as exosomes, which are lumenal MVB vesicles released from cells when MVBs fuse with the plasma membrane rather than lysosomes ;.

In light of the role that Bro1 has in facilitating MVB cargo deubiquitylation in yeast , it seems plausible to suspect that Alix might have a similar function promoting deubiquitylation at the site of viral assembly.