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J. Biol. Chem., Vol. 277, Issue 43, 41240-41246, October 25, 2002
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From the § Division of Geographic Medicine and the
Membrane skeletons play an important role in the
maintenance of cell shape and integrity in many cell types. In the
protozoan parasite Toxoplasma gondii this function is
performed by the subpellicular network, a resilient structure composed
of tightly interwoven 10-nm filaments. We report here that this network
is assembled at an early stage in the development of daughter
parasites. The networks of immature and mature parasites differ
dramatically with respect to their stability. Although in immature
parasites the network is completely solubilized by detergent, the
network in mature parasites is entirely detergent-resistant. Conversion of the detergent-labile to the detergent-resistant network occurs late
in daughter cell development and appears to be coupled to proteolytic
processing of the carboxyl terminus of TgIMC1, the major subunit of the
network filaments. A single cysteine residue in the TgIMC1 carboxyl
terminus was found to be essential for this processing event. The
dramatic change in resistance to detergent extraction probably reflects
an overall change in structural stability of the subpellicular network
that accompanies maturation of daughter parasites and allows a switch
from an assembly-competent but loose structure to one that is rigid and
offers mechanical strength to the mature parasite.
Proteolytic Processing of TgIMC1 during Maturation of the
Membrane Skeleton of Toxoplasma gondii*
,§¶
Department of Cell Biology, University of Alabama at
Birmingham, Birmingham, Alabama 35294-2170
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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