ArticleThe Biochemical journal2004
Characterization of a calmodulin-regulated Ca2+-dependent-protein-kinase-related protein kinase, AtCRK1, from Arabidopsis.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Beyond NPK: Mineral Nutrient-Mediated Modulation in Orchestrating Flowering Time.Plants (Basel, Switzerland) · 2023Review
- Calcium-dependent protein kinase 29 modulates PIN-FORMED polarity and Arabidopsis development via its own phosphorylation code.The Plant cell · 2021Article
- Functional Analysis of theInternational journal of molecular sciences · 2018Article
- Autophosphorylation-based Calcium (CaThe Journal of biological chemistry · 2017Article
- Calcium-dependent protein kinase (CDPK) and CDPK-related kinase (CRK) gene families in tomato: genome-wide identification and functional analyses in disease resistance.Molecular genetics and genomics : MGG · 2016Article
- Involvement of calmodulin and calmodulin-like proteins in plant responses to abiotic stresses.Frontiers in plant science · 2015Review
- Recent advances in calcium/calmodulin-mediated signaling with an emphasis on plant-microbe interactions.Plant physiology · 2013Review
- Inactivation of plasma membrane-localized CDPK-RELATED KINASE5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis.The Plant cell · 2013Article
- Article
- Expressional analysis and role of calcium regulated kinases in abiotic stress signaling.Current genomics · 2010Article
- Molecular and genetic evidence for the key role of AtCaM3 in heat-shock signal transduction in Arabidopsis.Plant physiology · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An AtCRK1 [Arabidopsis thaliana CDPK (Ca2+-dependent protein kinase)-related protein kinase 1] has been characterized molecularly and biochemically. AtCRK1 contains the kinase catalytic domain and a CaM (calmodulin)-binding site. Our results demonstrated that AtCRK1 could bind CaM in a Ca2+-dependent manner. This kinase phosphorylated itself and substrates such as histone IIIS and syntide-2 in a Ca2+-independent manner and the activity was stimulated by several CaM isoforms through its CaM-binding domain. This domain was localized within a stretch of 39 amino acid residues at positions from 403 to 441 with K(d)=67 nM for CaM binding. However, the stimulation amplification of the kinase activity of AtCRK1 by different CaM isoforms was similar.
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