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

. 2010 Mar 5;285(18):13839–13849. doi: 10.1074/jbc.M109.097345

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

© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

FIGURE 3. — The coiled-coil domain is critical for VAP-B oligomerization. Deletion of the coiled-coil (ΔCC) domain markedly reduces VAP-B oligomerization and together with the II mutant apparently abolishes VAP-B homo- (A) and hetero-dimerization (B) as determined by cross-linking experiments (A) and coimmunoprecipitation studies (B), respectively. C, deletion of the coiled-coil domain has no effect on Nir2 binding. The indicated Myc-tagged VAP-B proteins were co-expressed with HA-tagged Nir2, and their association was assessed by immunoprecipitation using anti-Myc antibody following by immunoblotting using anti-HA antibody. D, the indicated Myc-tagged VAP-B proteins were expressed in HeLa cells either alone or together with HA-tagged Nir2. The localization of the indicated proteins was determined by indirect immunofluorescence analysis. Representative confocal images demonstrating the formation of stacked ER-membrane arrays upon co-expression with Nir2 are shown in the lower panels. Scale bar, 10 μm.