Fbx15 interacts with the transcriptional repressor subunit SsnF without affecting its stability.


<p>(A) Scheme of a subset of interacting proteins of Fbx15 and SconB based on LC-MS/MS identifications. Shown are presumably nuclear proteins, which are either exclusively found for each F-box protein or which were found for both. Further Fbx15-TAP co-purified proteins included three CSN subunits and the cyclin-dependent kinase NimX. (B) BiFC of Fbx15 and SsnF showed a predominantly cytoplasmic YFP-signal, whereas unphosphorylated Fbx15[S468|9A] interacted with SsnF primarily in the nucleus. (C) Protein stability assays of SsnF-GFP in wild type, Δ<i>fbx15</i> or <i>fbx15</i> overexpression backgrounds with cultures exposed to cycloheximide (CHX) showed no Fbx15-dependent SsnF stability changes.</p

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oai:figshare.com:article/3843180Last time updated on 2/12/2018

This paper was published in FigShare.

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