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

. 2014 Oct 23;3:e03766. doi: 10.7554/eLife.03766

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

This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication.

PMC Copyright notice

Figure 5. — (A) AtLYK5 associates with AtCERK1 after chitin treatments. HA-tagged AtCERK1 and Myc-tagged AtLYK5 or AtCERK1 were co-expressed in protoplasts made from Col-0 wild-type plants. Protoplasts were harvested with or without the treatment with 1 µM chitooctaose as labeled above. Co-immunoprecipitation was made using anti-Myc antibody. Left panel and right panel are cropped from the same gel. (B) The association between AtCERK1 and AtLYK5 is induced by different chitin oligomers. Protoplasts were treated with different chitin oligomers (1 µM) as shown above for 15 min. (C) AtLYK5 regulates chitin-induced AtCERK1-AtCERK1 association. HA-tagged AtCERK1 and Myc-tagged AtCERK1 were copexpressed in protoplasts made from Col-0 wild-type or Atlyk5-2 mutant plants. Protoplasts were harvested with or without the treatment with 1 µM chitooctaose. Co-immunoprecipitation was made using anti-Myc antibody. (D) AtLYK5 controls chitin-induced phosphorylation of AtCERK1. Plant leaves from wild-type and the Atlyk5-2 mutant plants were treated with 1 µM chitooctaose for the time shown above. Anti-AtCERK1 antibody was used to detect the phosphorylation status of AtCERK1 shown as a shift in protein migration. Lower panel shows a non-specific band used to assess similar loading of each lane.

DOI: http://dx.doi.org/10.7554/eLife.03766.016

Figure 5—figure supplement 1. — (A) AtLYK5 associates with AtCERK1 after chitin treatments. HA-tagged AtCERK1 and Myc-tagged AtLYK5 or AtCERK1 were co-expressed in protoplasts made from Col-0 wild-type plants. Protoplasts were harvested with or without the treatment with 1 µM chitooctaose as labeled above. Co-immunoprecipitation was made using anti-Myc antibody. Left panel and right panel are cropped from the same gel. (B) The association between AtCERK1 and AtLYK5 is induced by different chitin oligomers. Protoplasts were treated with different chitin oligomers (1 µM) as shown above for 15 min. (C) AtLYK5 regulates chitin-induced AtCERK1-AtCERK1 association. HA-tagged AtCERK1 and Myc-tagged AtCERK1 were copexpressed in protoplasts made from Col-0 wild-type or Atlyk5-2 mutant plants. Protoplasts were harvested with or without the treatment with 1 µM chitooctaose. Co-immunoprecipitation was made using anti-Myc antibody. (D) AtLYK5 controls chitin-induced phosphorylation of AtCERK1. Plant leaves from wild-type and the Atlyk5-2 mutant plants were treated with 1 µM chitooctaose for the time shown above. Anti-AtCERK1 antibody was used to detect the phosphorylation status of AtCERK1 shown as a shift in protein migration. Lower panel shows a non-specific band used to assess similar loading of each lane.

DOI: http://dx.doi.org/10.7554/eLife.03766.016