Document Detail

Structural and functional characterization of the protein kinase Mps1 in Arabidopsis thaliana.
MedLine Citation:
PMID:  23049844     Owner:  NLM     Status:  MEDLINE    
In eukaryotes, protein kinases catalyze the transfer of a gamma-phosphate from ATP (or GTP) to specific amino acids in protein targets. In plants, protein kinases have been shown to participate in signaling cascades driving responses to environmental stimuli and developmental processes. Plant meristems are undifferentiated tissues that provide the major source of cells that will form organs throughout development. However, non-dividing specialized cells can also dedifferentiate and re-initiate cell division if exposed to appropriate conditions. Mps1 (Monopolar spindle) is a dual-specificity protein kinase that plays a critical role in monitoring the accuracy of chromosome segregation in the mitotic checkpoint mechanism. Although Mps1 functions have been clearly demonstrated in animals and fungi, its role in plants is so far unclear. Here, using structural and biochemical analyses here we show that Mps1 has highly similar homologs in many plant genomes across distinct lineages (e.g. AtMps1 in Arabidopsis thaliana). Several structural features (i.e. catalytic site, DFG motif and threonine triad) are clearly conserved in plant Mps1 kinases. Structural and sequence analysis also suggest that AtMps1 interact with other cell cycle proteins, such as Mad2 and MAPK1. By using a very specific Mps1 inhibitor (SP600125) we show that compromised AtMps1 activity hampers the development of A. thaliana seedlings in a dose-dependent manner, especially in secondary roots. Moreover, concomitant administration of the auxin IAA neutralizes the AtMps1 inhibition phenotype, allowing secondary root development. These observations let us to hypothesize that AtMps1 might be a downstream regulator of IAA signaling in the formation of secondary roots. Our results indicate that Mps1 might be a universal component of the Spindle Assembly Checkpoint machinery across very distant lineages of eukaryotes.
Eduardo Alves Gamosa de Oliveira; Nelilma Correia Romeiro; Elane da Silva Ribeiro; Claudete Santa-Catarina; Antônia Elenir Amâncio Oliveira; Vanildo Silveira; Gonçalo Apolinário de Souza Filho; Thiago Motta Venancio; Marco Antônio Lopes Cruz
Related Documents :
23229854 - Gallotannin causes differentiation and inflammation via erk‑1/‑2 and p38 kinase pat...
8883084 - Ferricyanide reductase activity in cataractous human lens.
2250564 - Effect of spermine on association of protein kinase c with phospholipid vesicles.
2392194 - Regulation of ornithine decarboxylase in rat kidney.
2165444 - Phospholamban and troponin i are substrates for protein kinase c in vitro but not in in...
8407944 - Regulation of epidermal growth factor receptor in nih3t3/her14 cells by antireceptor mo...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-26
Journal Detail:
Title:  PloS one     Volume:  7     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2012  
Date Detail:
Created Date:  2012-10-10     Completed Date:  2013-05-07     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e45707     Citation Subset:  IM    
Laboratório de Biotecnologia Vegetal, Núcleo em Ecologia e Desenvolvimento Sócio-ambiental de Macaé, Universidade Federal do Rio de Janeiro, Macaé, Rio de Janeiro, Brazil.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Motifs
Amino Acid Sequence
Arabidopsis / metabolism*
Arabidopsis Proteins / chemistry*
Cell Cycle Proteins / chemistry*
Enzyme Inhibitors / pharmacology
Evolution, Molecular
Gene Expression Regulation, Plant*
Genome, Plant
Molecular Conformation
Molecular Sequence Data
Plant Roots / metabolism
Protein Kinases / chemistry*
Protein-Serine-Threonine Kinases / chemistry*
Protein-Tyrosine Kinases / chemistry*
Sequence Homology, Amino Acid
Signal Transduction
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Cell Cycle Proteins; 0/Enzyme Inhibitors; EC 2.7.-/Mps1 protein, Arabidopsis; EC 2.7.-/Protein Kinases; EC Kinases; EC Kinases; EC protein, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  IL-27-induced gene expression is downregulated in HIV-infected subjects.
Next Document:  The CaMK4/CREB/IRS-2 cascade stimulates proliferation and inhibits apoptosis of ?-cells.