This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 19/9/2804    most recent tpc.107.051870v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in Plant Cell Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via ISI Web of Science (6) Citing Articles via Google Scholar Google Scholar Articles by Pierre, M. Articles by Meinnel, T. Search for Related Content PubMed PubMed Citation Articles by Pierre, M. Articles by Meinnel, T. Agricola Articles by Pierre, M. Articles by Meinnel, T.

N-Myristoylation Regulates the SnRK1 Pathway in Arabidopsis^[W]

^a Protein Maturation and Cell Fate, Institut des Sciences du Végétal, Unité Propre de Recherche 2355, Centre National de la Recherche Scientifique, F-91198 Gif-sur-Yvette cedex, France
^b Institut de Biotechnologie des Plantes, Unité Mixte de Recherche 8618, Centre National de la Recherche Scientifique, Univ Paris-Sud, 91405 Orsay cedex, France
^c Station de Génétique et d'Amélioration des Plantes, Institut National de la Recherche Agronomique, F-78026 Versailles Cedex, France

² Address correspondence to thierry.meinnel{at}isv.cnrs-gif.fr.

Cotranslational and posttranslational modifications are increasingly recognized as important in the regulation of numerous essential cellular functions. N-myristoylation is a lipid modification ensuring the proper function and intracellular trafficking of proteins involved in many signaling pathways. Arabidopsis thaliana, like human, has two tightly regulated N-myristoyltransferase (NMT) genes, NMT1 and NMT2. Characterization of knockout mutants showed that NMT1 was strictly required for plant viability, whereas NMT2 accelerated flowering. NMT1 impairment induced extremely severe defects in the shoot apical meristem during embryonic development, causing growth arrest after germination. A transgenic plant line with an inducible NMT1 gene demonstrated that NMT1 expression had further effects at later stages. NMT2 did not compensate for NMT1 in the nmt1-1 mutant, but NMT2 overexpression resulted in shoot and root meristem abnormalities. Various data from complementation experiments in the nmt1-1 background, using either yeast or human NMTs, demonstrated a functional link between the developmental arrest of nmt1-1 mutants and the myristoylation state of an extremely small set of protein targets. We show here that protein N-myristoylation is systematically associated with shoot meristem development and that SnRK1 (for SNF1-related kinase) is one of its essential primary targets.

Related articles in Plant Cell:

Shoot Meristem Development Depends on N-Myristoylation of SnRK1

Nancy A. Eckardt
Plant Cell 2007 19: 2703. [Full Text]  

This article has been cited by other articles:

				Y. Zhang, L. F. Primavesi, D. Jhurreea, P. J. Andralojc, R. A.C. Mitchell, S. J. Powers, H. Schluepmann, T. Delatte, A. Wingler, and M. J. Paul Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate Plant Physiology, April 1, 2009; 149(4): 1860 - 1871. [Abstract] [Full Text] [PDF]

				E. A. Ananieva, G. E. Gillaspy, A. Ely, R. N. Burnette, and F. L. Erickson Interaction of the WD40 Domain of a Myoinositol Polyphosphate 5-Phosphatase with SnRK1 Links Inositol, Sugar, and Stress Signaling Plant Physiology, December 1, 2008; 148(4): 1868 - 1882. [Abstract] [Full Text] [PDF]

				C. Polge, M. Jossier, P. Crozet, L. Gissot, and M. Thomas {beta}-Subunits of the SnRK1 Complexes Share a Common Ancestral Function Together with Expression and Function Specificities; Physical Interaction with Nitrate Reductase Specifically Occurs via AKIN{beta}1-Subunit Plant Physiology, November 1, 2008; 148(3): 1570 - 1582. [Abstract] [Full Text] [PDF]