GIGANTEA recruits the UBP12 and UBP13 deubiquitylases to regulate accumulation of the ZTL photoreceptor complex
Sign Up to like & getrecommendations! Published in 2019 at "Nature Communications"
DOI: 10.1038/s41467-019-11769-7
Abstract: ZEITLUPE (ZTL), a photoreceptor with E3 ubiquitin ligase activity, communicates end-of-day light conditions to the plant circadian clock. It still remains unclear how ZTL protein accumulates in the light but does not destabilize target proteins… read more here.
Keywords: gigantea recruits; photoreceptor complex; ztl; ztl photoreceptor ... See more keywords
The deubiquitinases UBP12 and UBP13 integrate with the E3 ubiquitin ligase XBAT35.2 to modulate VPS23A stability in ABA signaling
Sign Up to like & getrecommendations! Published in 2022 at "Science Advances"
DOI: 10.1126/sciadv.abl5765
Abstract: Ubiquitination-mediated protein degradation in both the 26S proteasome and vacuole is an important process in abscisic acid (ABA) signaling. However, the role of deubiquitination in this process remains elusive. Here, we demonstrate that two deubiquitinating… read more here.
Keywords: vps23a; aba signaling; modulate; stability aba ... See more keywords
Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1
Sign Up to like & getrecommendations! Published in 2022 at "EMBO reports"
DOI: 10.15252/embr.202153354
Abstract: Protein ubiquitination is a dynamic and reversible post‐translational modification that controls diverse cellular processes in eukaryotes. Ubiquitin‐dependent internalization, recycling, and degradation are important mechanisms that regulate the activity and the abundance of plasma membrane (PM)‐localized… read more here.
Keywords: bri1; enzymes ubp12; deubiquitinating enzymes; ubp12 ubp13 ... See more keywords