SGD Paper 
Fries T, et al. (2011) The Saccharomyces cerevisiae ubiquitin E3 ligase Asr1p targets calmodulin for ubiquitylation. Biochem Biophys Res Commun 411(1):197-201
Abstract: Yeast calmodulin known to be ubiquitylated in vivo in a Ca(2+) dependent manner has long remained an orphan substrate. Here we identify Saccharomyces cerevisiae Asr1p as an ubiquitin E3 ligase for yeast calmodulin, a protein involved in calcium signaling. A short region within Asr1p-C harboring two putative calmodulin-binding motifs is sufficient and necessary for interaction with calmodulin. The interaction is direct, occurs in vivo and depends on physiological concentrations of Ca(2+). A minimal set of purified proteins including Asr1p E3 ligase was sufficient for in vitro ubiquitylation of calmodulin, a reaction that required a functional Asr1p Ring domain. We propose a role of the Asr1p E3 ligase activity in coping with stress.
| Status: Published | Type: Journal Article | PubMed ID: 21726536 |
Topics addressed in this paper
Number of different genes curated to this paper: 3
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