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How does TRIP12 interact with dcaf7? 


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TRIP12 interacts with DCAF7 by mediating branched K11-linked ubiquitylation of FBW7, regulating its stability and affecting the abundance of SCFFBW7 substrates . Additionally, DCAF7, also known as WDR68, binds DYRK1A and DYRK1B, playing a crucial role in maintaining normal levels of these kinases . Furthermore, Trip12 is involved in the ubiquitination of Sox6, a transcription factor in muscle cells, leading to its polyubiquitination and subsequent degradation via the ubiquitin-proteasome system . These interactions highlight the diverse roles of TRIP12 in regulating the stability and activity of various proteins involved in critical cellular processes.

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