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Regulation of the Plasmodium motor complex: Phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA

Lookup NU author(s): Professor Paula SalgadoORCiD

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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 Apicomplexa parasites. Recent data indicate that MTIP Ser107 and/or Ser108 are targeted for intracellular phosphorylation. Using an optimised 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, whilst S107E has a smaller but measurable impact. These data are consistent with physical interactions observed between recombinant MTIP and native MyoA from P. 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.

Publication metadata

Author(s): Douse CH, Green JL, Salgado PS, Simpson PJ, Thomas JC, Langsley G, Holder AA, Tate EW, Cota E

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 2012

Volume: 287

Issue: 44

Pages: 36968-36977

Print publication date: 29/08/2012

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: 10.1074/jbc.M112.379842

URL: http://dx.doi.org/10.1074/jbc.M112.379842

DOI: 10.1074/jbc.M112.379842

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