Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

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

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 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/).

PMC Copyright notice

Figure 4. — Fusion of DUbs to ESCRT proteins inhibits their ubiquitination but allows vacuolar sorting of Ub fusion cargo proteins. (A) Schematic of the ESCRT sorting apparatus showing subunits fused to different DUb catalytic domains. (B) Cells expressing myc-Ub and either Hse1-UL36-HA or Hse1-ul36*-HA (inactive) were transformed with vector alone or with plasmids expressing HA-Vps27. Lysates were immunoprecipitated (IP) with anti-HA antibodies. Immunoprecipitates were immunoblotted (IB) for HA (top) to confirm isolation of HA-tagged proteins; immunoprecipitates were immunoblotted with anti-myc to assess ubiquitination. Fusion of active UL36 abolished ubiquitination of either HA-tagged Hse1 or Vps27 proteins. Black lines indicate that dividing lanes have been spliced out. (C) ESCRT subunits, GGA, or His3 fused to the indicated active (Ubp7 or UL36) or inactive (ubp7* or ul36*) catalytic domains (CD) were expressed in wild-type cells. Cells coexpressed the indicated GFP-tagged MVB cargo. Bar, 6 µm.