کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2052265 | 1074225 | 2005 | 6 صفحه PDF | دانلود رایگان |
Calmodulin (CaM), a key Ca2+ sensor in eukaryotes, regulates diverse cellular processes by interacting with many proteins. To identify Ca2+/CaM-mediated signaling components, we screened an Arabidopsis expression library with horseradish peroxidase-conjugated Arabidopsis calmodulin2 (AtCaM2) and isolated a homolog of the UBP6 deubiquitinating enzyme family (AtUBP6) containing a Ca2+-dependent CaM-binding domain (CaMBD). The CaM-binding activity of the AtUBP6 CaMBD was confirmed by CaM mobility shift assay, phosphodiesterase competition assay and site-directed mutagenesis. Furthermore, expression of AtUBP6 restored canavanine resistance to the Δubp6 yeast mutant. This is the first demonstration that Ca2+ signaling via CaM is involved in ubiquitin-mediated protein degradation and/or stabilization in plants.
Journal: FEBS Letters - Volume 579, Issue 18, 18 July 2005, Pages 3885–3890