ArticleThe EMBO journal2001
The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.
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153 citing papers in PubMed, 412 citations in OpenAlex.
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- The role of CBL-CIPK signaling in plant responses to biotic and abiotic stresses.Plant molecular biology · 2024Review
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- Phytochromes enhance SOS2-mediated PIF1 and PIF3 phosphorylation and degradation to promote Arabidopsis salt tolerance.The Plant cell · 2023Article
- CIPK-B is essential for salt stress signalling in Marchantia polymorpha.The New phytologist · 2023Article
- Cold-induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice.The EMBO journal · 2023Article
- Functional identification of the calcineurin B-like protein PavCBL4 in modulating salt tolerance in sweet cherry.Frontiers in plant science · 2023Article
- Comprehensive identification and expression analyses of the SnRK gene family in Casuarina equisetifolia in response to salt stress.BMC plant biology · 2022Article
- Does Potassium (KInternational journal of molecular sciences · 2022Review
- Evolution of the CBL and CIPK gene families in Medicago: genome-wide characterization, pervasive duplication, and expression pattern under salt and drought stress.BMC plant biology · 2022Article
93 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arabidopsis calcineurin B-like calcium sensor proteins (AtCBLs) interact with a group of serine-threonine protein kinases (AtCIPKs) in a calcium-dependent manner. Here we identify a 24 amino acid domain (NAF domain) unique to these kinases as being required and sufficient for interaction with all known AtCBLs. Mutation of conserved residues either abolished or significantly diminished the affinity of AtCIPK1 for AtCBL2. Comprehensive two-hybrid screens with various AtCBLs identified 15 CIPKs as potential targets of CBL proteins. Database analyses revealed additional kinases from Arabidopsis and other plant species harbouring the NAF interaction module. Several of these kinases have been implicated in various signalling pathways mediating responses to stress, hormones and environmental cues. Full-length CIPKs show preferential interaction with distinct CBLs in yeast and in vitro assays. Our findings suggest differential interaction affinity as one of the mechanisms generating the temporal and spatial specificity of calcium signals within plant cells and that different combinations of CBL-CIPK proteins contribute to the complex network that connects various extracellular signals to defined cellular responses.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.