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Vol. 20, Issue 14, 3200-3208, July 15, 2009

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Dephosphorylation of Major Sperm Protein (MSP) Fiber Protein 3 by Protein Phosphatase 2A during Cell Body Retraction in the MSP-based Amoeboid Motility of Ascaris Sperm

Kexi Yi^*, Xu Wang^,, Mark R. Emmett^,, Alan G. Marshall^,, Murray Stewart, and Thomas M. Roberts^*

Departments of *Biological Science and Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306; Ion Cyclotron Resonance Program, National High Magnetic Field Laboratory, Tallahassee, FL 32310-4005; and Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom

Submitted March 24, 2009; Accepted May 13, 2009
Monitoring Editor: Paul Forscher

The crawling movement of nematode sperm requires coordination of leading edge protrusion with cell body retraction, both of which are powered by modulation of a cytoskeleton based on major sperm protein (MSP) filaments. We used a cell-free in vitro motility system in which both protrusion and retraction can be reconstituted, to identify two proteins involved in cell body retraction. Pharmacological and depletion-add back assays showed that retraction was triggered by a putative protein phosphatase 2A (PP2A, a Ser/Thr phosphatase activated by tyrosine dephosphorylation). Immunofluorescence showed that PP2A was present in the cell body and was concentrated at the base of the lamellipod where the force for retraction is generated. PP2A targeted MSP fiber protein 3 (MFP3), a protein unique to nematode sperm that binds to the MSP filaments in the motility apparatus. Dephosphorylation of MFP3 caused its release from the cytoskeleton and generated filament disassembly. Our results suggest that interaction between PP2A and MFP3 leads to local disassembly of the MSP cytoskeleton at the base of the lamellipod in sperm that in turn pulls the trailing cell body forward.

Address correspondence to: Thomas M. Roberts (roberts{at}bio.fsu.edu)