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. 2010 May 17;5(5):e10665. doi: 10.1371/journal.pone.0010665

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Spicer et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Yeast two two-hybrid assays were conducted using α5, α6 and αV cytoplasmic domains as bait in combination with kermit2 or kermit2_mut as prey. The data is presented as average normalized β-galactosidase activity (±SD). The interaction of kermit2 with α5 and α6 is abolished by the AEEL mutation in kermit2_mut (* P<0.002). The αV subunit does not interact with kermit2 or kermit2_mut (** indicates P<0.001 between α5 or α6 and αV bait constructs). (B) GST pulldowns. HA tagged Kermit2 is detected in lysates (lane 1 input), and is pulled down with a GST-α5 fusion construct (lane 2 GST-α5). Most of the kermit2 remains in the supernatant (lane 3 sup). A control GST-β1 construct (lane 5 GST-β1) does not pull Kermit2 from lysates (lane 4 input, lane 6 sup). (C) Coimmunoprecipitation of kermit2 with α5β1 integrin. HA tagged kermit2 is detected in lysates (lane 1 input). Kermit2 is found in association with immunoprecipitated α5β1 (lane 2 P8D4), while a significant portion of kermit2 remains in the supernatant (sup).