Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting |
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Authors: | Babst Markus Katzmann David J Estepa-Sabal Eden J Meerloo Timo Emr Scott D |
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Institution: | Department of Cellular and Molecular Medicine and Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, La Jolla 92093, USA. |
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Abstract: | The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes. |
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