Unusual anchor of a motor complex (MyoD-MLC2) to the plasma membrane of Toxoplasma gondii

Traffic. 2010 Dec 9. doi: 10.1111/j.1600-0854.2010.01148.x. [Epub ahead of print]

Unusual anchor of a motor complex (MyoD-MLC2) to the plasma membrane of Toxoplasma gondii

Polonais V, Foth BJ, Chinthalapudi K, Marq JB, Manstein DJ, Soldati-Favre D, Frénal K.

Department of Microbiology and Molecular Medicine, CMU, University of Geneva, 1 Rue Michel-Servet, CH-1211 Geneva 4, Switzerland Research Division for Structural Analysis, Hannover Medical School, OE8830, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany Institute für Biophysical Chemistry, Hannover Medical School, OE4350, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany.

Abstract
Toxoplasma gondii possesses 11 rather atypical myosin heavy chains. The only myosin light chain described to date is MLC1, associated to myosin A, and contributing to gliding motility. In this study, we examined the repertoire of calmodulin-like proteins in Apicomplexans, identified six putative myosin light chains and determined their subcellular localization in T. gondii and Plasmodium falciparum. MLC2, only found in coccidians, is associated to myosin D via its CaM-like domain and anchored to the plasma membrane of T. gondii via its N-terminal extension. Molecular modeling suggests that MyoD-MLC2 complex is more compact than the reported structure of Plasmodium MyoA-MTIP complex. Anchorage of this MLC2 to the plasma membrane is likely governed by palmitoylation.

© 2010 John Wiley & Sons A/S.
PMID: 21143563 [PubMed - as supplied by publisher]