Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2010 Jun;73(3):325-38.
doi: 10.1007/s11103-010-9617-4. Epub 2010 Mar 4.

TMKP1 is a novel wheat stress responsive MAP Kinase phosphatase localized in the nucleus

Ikram Zaïdi  1 , Chantal Ebel, Majdi Touzri, Etienne Herzog, Jean-Luc Evrard, Anne Catherine Schmit, Khaled Masmoudi, Moez Hanin
Affiliations

TMKP1 is a novel wheat stress responsive MAP Kinase phosphatase localized in the nucleus

Ikram Zaïdi et al. Plant Mol Biol. 2010 Jun.

Abstract

The regulation of plant signalling responses by Mitogen-Activated Protein Kinases (MAPKs)-mediated protein phosphorylation is well recognized. MAP kinase phosphatases (MKPs) are negative regulators of MAPKs in eukaryotes. We report here the identification and the characterization of TMKP1, the first wheat MKP (Triticum turgidum L. subsp. Durum). Expression profile analyses performed in two durum wheat cultivars showing a marked difference in salt and drought stress tolerance, revealed a differential regulation of TMKP1. Under salt and osmotic stress, TMKP1 is induced in the sensitive wheat variety and repressed in the tolerant one. A recombinant TMKP1 was shown to be an active phosphatase and capable to interact specifically with two wheat MAPKs (TMPK3 and TMPK6). In BY2 tobacco cells transiently expressing GFP::TMKP1, the fusion protein was localized into the nucleus. Interestingly, the deletion of the N-terminal non catalytic domain results in a strong accumulation of the truncated fusion protein in the cytoplasm. In addition, when expressed in BY2 cells, TMPK3 and TMPK6 fused to red fluorescent protein (RFP) were shown to be present predominantly in the nucleus. Surprisingly, when co-expressed with the N-terminal truncated TMKP1 fusion protein; both kinases are excluded from the nuclear compartment and accumulate in the cytoplasm. This strongly suggests that TMKP1 interacts in vivo with TMPK3 and TMPK6 and controls their subcellular localization. Taken together, our results show that the newly isolated wheat MKP might play an active role in modulating the plant cell responses to salt and osmotic stress responses.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Plant J. 2000 Dec;24(5):655-65 - PubMed
    1. Eur J Biochem. 2003 Aug;270(16):3291-9 - PubMed
    1. J Biol Chem. 2004 Jan 9;279(2):848-58 - PubMed
    1. Plant Cell Physiol. 2007 Feb;48(2):332-44 - PubMed
    1. J Cell Sci. 2005 Aug 15;118(Pt 16):3569-72 - PubMed

Publication types

MeSH terms

Associated data

LinkOut - more resources