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Author Johnson, Kim Leonie ♦ Faulkner, Christine ♦ Jeffree, Chris Edward ♦ Ingram, Gwyneth Christina
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher American Society of Plant Biologists
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Genetics and evolution ♦ Natural history of organisms ♦ Technology ♦ Medicine & health ♦ Human anatomy, cytology, histology ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Cells ♦ Plant Structures ♦ Anatomy ♦ Eukaryota ♦ Organisms ♦ Enzymes and Coenzymes ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Cell Physiological Phenomena ♦ Genetic Phenomena ♦ Biological Sciences
Subject Keyword Discipline Botany ♦ Arabidopsis Proteins ♦ Physiology ♦ Arabidopsis ♦ Enzymology ♦ Calpain ♦ Genetics ♦ Growth & Development ♦ Analysis ♦ Chemistry ♦ Cell Membrane ♦ Cell Proliferation ♦ Cytoplasm ♦ Endoplasmic Reticulum ♦ Enzyme Activation ♦ Genetic Complementation Test ♦ Green Fluorescent Proteins ♦ Meristem ♦ Mutation ♦ Phenotype ♦ Plant Leaves ♦ Metabolism ♦ Protein Structure, Tertiary ♦ Recombinant Fusion Proteins ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract The role of the unique plant calpain Defective Kernel 1 (DEK1) in development has remained unclear due to the severity of mutant phenotypes. Here, we used complementation studies of the embryo-lethal mutant to dissect DEK1 protein behavior and to show that DEK1 plays a key role in growth regulation in Arabidopsis thaliana. We show that although full-length DEK1 protein localizes to membranes, it undergoes intramolecular autolytic cleavage events that release the calpain domain into the cytoplasm. The active calpain domain alone is not only necessary for DEK1 function but is sufficient for full complementation of dek1 mutants. A novel set of phenotypes, including leaf ruffling, increased leaf thickness, and abnormalities of epidermal cell interdigitation, was caused by expression of the constitutively active calpain domain. This analysis of the novel phenotypes produced by DEK1 under- and overexpression, as well as DEK1 subcellular localization and protein processing, has revealed a fundamental role for DEK1-mediated signaling in growth regulation.
Description Country affiliation: United kingdom
Author Affiliation: Johnson KL ( Institute of Molecular Plant Sciences, Kings Buildings, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.)
ISSN 10404651
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2008-10-01
Publisher Place United States
e-ISSN 1531298X
Volume Number 20
Issue Number 10

Source: WHO-Global Index Medicus