title: Localized depolymerization of the major sperm protein cytoskeleton correlates with the forward movement of the cell body in the amoeboid movement of nematode sperm.
abstract: 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.
authors.affiliation: Department of Biological Science, Florida State University, Tallahassee, Florida 32306, USA.
authors.forename: J E
authors.initials: JE
authors.lastname: Italiano
authors.forename: M
authors.initials: M
authors.lastname: Stewart
authors.forename: T M
authors.initials: TM
authors.lastname: Roberts
mesh_terms: D008841:Actin Cytoskeleton / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D001152:Arsenicals / Q000037:antagonists & inhibitors / Q000494:pharmacology; D017165:Ascaris suum / Q000166:cytology*; D002448:Cell Adhesion; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D048429:Cell Size / Q000187:drug effects; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism*; D005898:Glass; D015801:Helminth Proteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D011108:Polymers; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors; D011554:Pseudopodia / Q000187:drug effects / Q000378:metabolism; D013077:Sperm Head / Q000187:drug effects / Q000378:metabolism; D013081:Sperm Motility / Q000187:drug effects; D013094:Spermatozoa / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism
chemical_list: D001152:Arsenicals; D015801:Helminth Proteins; D011108:Polymers; C050602:major sperm protein, nematode; C029341:oxophenylarsine; D017027:Protein Tyrosine Phosphatases