ArticlePlant physiology2002
An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum.
Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 140 citations in OpenAlex.
- Calcium-Dependent Protein Kinases in Plants: Structure, Signaling, and Multifaceted Regulatory Roles in Development and Stress Adaptation.International journal of molecular sciences · 2026Review
- CPK2 Enhances ABA Sensitivity in Seed Germination and Root Growth by Promoting ABA-InducedPlants (Basel, Switzerland) · 2025Article
- Interdependence of plasma membrane nanoscale dynamics of a kinase and its cognate substrate underlieseLife · 2025Article
- Whole-Genome Identification of Regulatory Function of CDPK Gene Families in Cold Stress Response forPlants (Basel, Switzerland) · 2023Article
- The Roles of CDPKs as a Convergence Point of Different Signaling Pathways in Maize Adaptation to Abiotic Stress.International journal of molecular sciences · 2023Review
- Identification and Expression Analysis of Calcium-Dependent Protein Kinases Gene Family in Potato Under Drought Stress.Frontiers in genetics · 2022Article
- Protein N-myristoylation: functions and mechanisms in control of innate immunity.Cellular & molecular immunology · 2021Review
- The Role of Calcium/Calcium-Dependent Protein Kinases Signal Pathway in Pollen Tube Growth.Frontiers in plant science · 2021Review
- Molecular cloning and expression of AmCDPK from mangrove Avicennia marina under elevated temperature.Ecotoxicology (London, England) · 2020Article
- Dynamic Protein S-Acylation in Plants.International journal of molecular sciences · 2019Review
- TheInternational journal of molecular sciences · 2018Review
- CaScientific reports · 2018Article
- Targeted Profiling ofThe Plant cell · 2018Article
- Calcium-dependent protein kinases in cotton: insights into early plant responses to salt stress.BMC plant biology · 2018Article
- Calcium-Dependent Protein Kinases in Phytohormone Signaling Pathways.International journal of molecular sciences · 2017Review
- Analysis of the potato calcium-dependent protein kinase family and characterization of StCDPK7, a member induced upon infection with Phytophthora infestans.Plant cell reports · 2017Article
- Calcium-dependent protein kinase OsCPK10 mediates both drought tolerance and blast disease resistance in rice plants.Journal of experimental botany · 2017Article
- Article
- Genome-wide identification of calcium-dependent protein kinases in soybean and analyses of their transcriptional responses to insect herbivory and drought stress.Scientific reports · 2016Article
- Genome-wide identification of Calcineurin B-Like (CBL) gene family of plants reveals novel conserved motifs and evolutionary aspects in calcium signaling events.BMC plant biology · 2015Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arabidopsis contains 34 genes that are predicted to encode calcium-dependent protein kinases (CDPKs). CDPK enzymatic activity previously has been detected in many locations in plant cells, including the cytosol, the cytoskeleton, and the membrane fraction. However, little is known about the subcellular locations of individual CDPKs or the mechanisms involved in targeting them to those locations. We investigated the subcellular location of one Arabidopsis CDPK, AtCPK2, in detail. Membrane-associated AtCPK2 did not partition with the plasma membrane in a two-phase system. Sucrose gradient fractionation of microsomes demonstrated that AtCPK2 was associated with the endoplasmic reticulum (ER). AtCPK2 does not contain transmembrane domains or known ER-targeting signals, but does have predicted amino-terminal acylation sites. AtCPK2 was myristoylated in a cell-free extract and myristoylation was prevented by converting the glycine at the proposed site of myristate attachment to alanine (G2A). In plants, the G2A mutation decreased AtCPK2 membrane association by approximately 50%. A recombinant protein, consisting of the first 10 amino acids of AtCPK2 fused to the amino-terminus of beta-glucuronidase, was also targeted to the ER, indicating that the amino terminus of AtCPK2 can specify ER localization of a soluble protein. These results indicate that AtCPK2 is localized to the ER, that myristoylation is likely to be involved in the membrane association of AtCPK2, and that the amino terminal region of AtCPK2 is sufficient for correct membrane targeting.
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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.