Plant Cell Plant Cell 20th
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


First published online October 24, 2008; 10.1105/tpc.108.059964

The Plant Cell 20:2619-2630 (2008)
© 2008 American Society of Plant Biologists

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
20/10/2619    most recent
tpc.108.059964v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johnson, K. L.
Right arrow Articles by Ingram, G. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, K. L.
Right arrow Articles by Ingram, G. C.
Agricola
Right arrow Articles by Johnson, K. L.
Right arrow Articles by Ingram, G. C.

The Phytocalpain Defective Kernel 1 Is a Novel Arabidopsis Growth Regulator Whose Activity Is Regulated by Proteolytic Processing[W]

Kim Leonie Johnson, Christine Faulkner, Chris Edward Jeffree and Gwyneth Christina Ingram1

Institute of Molecular Plant Sciences, Kings Buildings, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom

1 Address correspondence to gwyneth.ingram{at}ed.ac.uk.

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.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 2008 by the American Society of Plant Biologists