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© The Rockefeller University Press, 0021-9525/1999//1087 $5.00
The Journal of Cell Biology, Volume 146, Number 5, , 1999 1087-1096

Original Article

Localized Depolymerization of the Major Sperm Protein Cytoskeleton Correlates with the Forward Movement of the Cell Body in the Amoeboid Movement of Nematode Sperm



Joseph E. Italiano, Jr.a, Murray Stewartb, and Thomas M. Robertsa

a Department of Biological Science, Florida State University, Tallahassee, Florida 32306
b Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom
Department of Biological Science, 336 Bio Unit I, Florida State University, Tallahassee, FL 32306.(850) 644-0481(850) 644-4424

roberts{at}bio.fsu.edu

The major sperm protein (MSP)-based amoeboid motility of Ascaris suum sperm requires coordinated lamellipodial protrusion and cell body retraction. In these cells, protrusion and retraction are tightly coupled to the assembly and disassembly of the cytoskeleton at opposite ends of the lamellipodium. Although polymerization along the leading edge appears to drive protrusion, the behavior of sperm tethered to the substrate showed that an additional force is required to pull the cell body forward. To examine the mechanism of cell body movement, we used pH to uncouple cytoskeletal polymerization and depolymerization. In sperm treated with pH 6.75 buffer, protrusion of the leading edge slowed dramatically while both cytoskeletal disassembly at the base of the lamellipodium and cell body retraction continued. At pH 6.35, the cytoskeleton pulled away from the leading edge and receded through the lamellipodium as its disassembly at the cell body continued. The cytoskeleton disassembled rapidly and completely in cells treated at pH 5.5, but reformed when the cells were washed with physiological buffer. Cytoskeletal reassembly occurred at the lamellipodial margin and caused membrane protrusion, but the cell body did not move until the cytoskeleton was rebuilt and depolymerization resumed. These results indicate that cell body retraction is mediated by tension in the cytoskeleton, correlated with MSP depolymerization at the base of the lamellipodium.

Key Words: amoeboid motility • retraction • major sperm protein • actin • lamellipodium

© 1999 The Rockefeller University Press

1.used in this paper: HKB-acetate, HKB buffer containing 20 mM sodium acetate; MSP, major sperm protein; PAO, phenylarsine oxide

Dr. Italiano's current address is Division of Hematology, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115.


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