Disease relevance of STP22

• A peptide sequence in this domain, PTVP, is involved in the function of Vps27 in the MVB pathway, the efficient endosomal recruitment of ESCRT-I, and is related to a motif in HIV-1 Gag protein that is capable of interacting with Tsg101, the mammalian homologue of Vps23 [1].

High impact information on STP22

• Vps27 also bound Vps23 directly via two PSDP motifs present within the Vps27 COOH terminus [2].
• Mutations gef1, stp22, STP26, and STP27 in Saccharomyces cerevisiae were identified as suppressors of the temperature-sensitive alpha-factor receptor (mutation ste2-3) and arginine permease (mutation can1(ts)) [3].
• In the stp22 mutant, both the mutant and the wild-type receptors (tagged with green fluorescent protein [GFP]) accumulated within an endosome-like compartment and were excluded from the vacuole [3].
• Here, we report that the Arabidopsis ELCH (ELC) gene encodes a Vps23p/TSG101 homolog, and that homologs of all known ESCRT I-III components are present in the Arabidopsis genome [4].
• It has been shown that ESCRT-I contains the vacuolar protein sorting (Vps) proteins Vps23, Vps28, and Vps37 [5].

Anatomical context of STP22

• The Saccharomyces cerevisiae VPS23 (STP22) gene is implicated in the control of vesicle movement and quality of plasma membrane proteins [6].

Other interactions of STP22

• Loss of Vps27-Vps23 association led to less efficient sorting into the endosomal lumen [2].

References