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. 2011 Jan 24;192(2):229–242. doi: 10.1083/jcb.201008121

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© 2011 Stringer and Piper

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — Vps27 lacking lysine residues is not ubiquitinated but still functions in MVB cargo sorting. (A) Ubiquitination of Vps27 was assessed in cells expressing HA-Vps27 and myc-Ub. Vps27 immunoprecipitates (IP) from denatured cell lysates were immunoblotted (IB) for HA-Vps27 (anti-HA) or Ub (anti-myc). Input represents a 5% equivalent. Black lines indicate that dividing lanes have been spliced out. (B) Domain organization of yeast ESCRT-0 protein Vps27. Blue lines show positions of the 47 lysines. (C) Ubiquitination of wild-type and lysine-less Vps27 (HA-Vps27^WT and HA-Vps27^K>R) was assessed in ubp2Δ cells expressing myc-Ub. Anti-HA (Vps27) immunoprecipitates (IP) were immunoblotted (IB) for HA-Vps27 (anti-HA) or Ub (anti-myc). Input represents a 5% equivalent. *, expected molecular weight; **, ubiquitinated forms. (D) Sorting of Ste3-GFP in vps27Δ, vps27Δ ubp2Δ, or vps27Δ hse1Δ (ESCRT-0Δ) cells transformed with plasmids expressing HA-Vps27^WT or HA-Vps27^K>R. Bar, 5 µm.