Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains
This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.
Comment:based on the binding of Alix to the YPXnL (n=1-3) late domains of HIV and EIAV; late domains are short peptide motifs found in viral Gag proteins
Comment:some members of this superfamily interact with nonviral YPXnL motifs; Saccharomyces cerevisiae Bro1 with a YPxL motif in Doa4
Jiyao W et al.(2023). "The conserved domain database in 2023.",