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Regulation of the Plasmodium Motor Complex: PHOSPHORYLATION OF MYOSIN A TAIL-INTERACTING PROTEIN (MTIP) LOOSENS ITS GRIP ON MyoA*
- Publication Year :
- 2012
- Publisher :
- American Society for Biochemistry and Molecular Biology, 2012.
-
Abstract
- The interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an essential feature of the conserved molecular machinery required for gliding motility and cell invasion by apicomplexan parasites. Recent data indicate that MTIP Ser-107 and/or Ser-108 are targeted for intracellular phosphorylation. Using an optimized MyoA tail peptide to reconstitute the complex, we show that this region of MTIP is an interaction hotspot using x-ray crystallography and NMR, and S107E and S108E mutants were generated to mimic the effect of phosphorylation. NMR relaxation experiments and other biophysical measurements indicate that the S108E mutation serves to break the tight clamp around the MyoA tail, whereas S107E has a smaller but measurable impact. These data are consistent with physical interactions observed between recombinant MTIP and native MyoA from Plasmodium falciparum lysates. Taken together these data support the notion that the conserved interactions between MTIP and MyoA may be specifically modulated by this post-translational modification.
- Subjects :
- Models, Molecular
Differential Thermal Analysis
Erythrocytes
Nonmuscle Myosin Type IIA
fungi
Plasmodium falciparum
Protozoan Proteins
Titrimetry
Crystallography, X-Ray
Protein Structure, Secondary
Protein Structure, Tertiary
Cytoskeletal Proteins
Amino Acid Substitution
parasitic diseases
Protein Structure and Folding
Humans
Thermodynamics
Fluorometry
Phosphorylation
Protein Structure, Quaternary
Protein Processing, Post-Translational
Cells, Cultured
Protein Binding
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.pmid..........f54bf5e0d4a142a128eeab0f0c25934a