1. Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with calmodulin
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Moon, Byeong Cheol, Choi, Man Soo, Kang, Yun Hwan, Kim, Min Chul, Cheong, Mi Sun, Park, Chan Young, Yoo, Jae Hyuk, Koo, Sung Cheol, Lee, Sang Min, Lim, Chae Oh, Cho, Moo Je, and Chung, Woo Sik
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CALMODULIN ,EUKARYOTIC cells ,ARABIDOPSIS ,HORSERADISH - Abstract
Abstract: Calmodulin (CaM), a key Ca
2+ 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. [Copyright &y& Elsevier]- Published
- 2005
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