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Citation

BibTex format

@article{Douse:2012:10.1074/jbc.M112.379842,
author = {Douse, CH and Green, JL and Salgado, PS and Simpson, PJ and Thomas, JC and Langsley, G and Holder, AA and Tate, EW and Cota, E},
doi = {10.1074/jbc.M112.379842},
journal = {Journal of Biological Chemistry},
pages = {36968--36977},
title = {Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.},
url = {http://dx.doi.org/10.1074/jbc.M112.379842},
volume = {287},
year = {2012}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Background: Recent phosphoproteome data reveal the extent of post-translational phosphorylation in selected apicomplexanparasites.Results: Binding site mutants that mimic the effect of MTIP phosphorylation in vivo severely decrease MyoA binding.Conclusion: Phosphorylation of selected binding site residues modulates the activity of the actomyosin motor.Significance: Study of Apicomplexa phosphosites can inform on the regulation of functions involved in pathogenesis.
AU  - Douse,CH
AU  - Green,JL
AU  - Salgado,PS
AU  - Simpson,PJ
AU  - Thomas,JC
AU  - Langsley,G
AU  - Holder,AA
AU  - Tate,EW
AU  - Cota,E
DO  - 10.1074/jbc.M112.379842
EP  - 36977
PY  - 2012///
SN  - 1083-351X
SP  - 36968
TI  - Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M112.379842
VL  - 287
ER  -
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Contact

Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ

e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821