Major Sperm Protein and Sperm Locomotion

Author(s):  
Katsuya Shimabukuro ◽  
Thomas M. Roberts ◽  
Vikash Verma
1999 ◽  
Vol 146 (5) ◽  
pp. 1087-1096 ◽  
Author(s):  
Joseph E. Italiano ◽  
Murray Stewart ◽  
Thomas M. Roberts

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.


1994 ◽  
Vol 107 (10) ◽  
pp. 2941-2949
Author(s):  
K.L. King ◽  
M. Stewart ◽  
T.M. Roberts

Sperm of the nematode, Ascaris suum, are amoeboid cells that do not require actin or myosin to crawl over solid substrata. In these cells, the role usually played by actin has been taken over by major sperm protein (MSP), which assembles into filaments that pack the sperm pseudopod. These MSP filaments are organized into multi-filament arrays called fiber complexes that flow centripetally from the leading edge of the pseudopod to the cell body in a pattern that is intimately associated with motility. We have characterized structurally a hierarchy of helical assemblies formed by MSP. The basic unit of the MSP cytoskeleton is a filament formed by two subfilaments coiled around one another along right-handed helical tracks. In vitro, higher-order assemblies (macrofibers) are formed by MSP filaments that coil around one another in a left-handed helical sense. The multi-filament assemblies formed by MSP in vitro are strikingly similar to the fiber complexes that characterize the sperm cytoskeleton. Thus, self-association is an intrinsic property of MSP filaments that distinguishes these fibers from actin filaments. The results obtained with MSP help clarify the roles of different aspects of the actin cytoskeleton in the generation of locomotion and, in particular, emphasize the contributions made by vectorial assembly and filament bundling.


2008 ◽  
Vol 103 (1) ◽  
pp. 11-20 ◽  
Author(s):  
Johan Höglund ◽  
Annie Engström ◽  
David A. Morrison ◽  
Anna Mineur ◽  
Jens G. Mattsson

2019 ◽  
Vol 197 ◽  
pp. 51-56 ◽  
Author(s):  
Lin Huang ◽  
Ping Wang ◽  
Min-Qi Tian ◽  
Li-Hua Zhu ◽  
Jian-Ren Ye

1996 ◽  
Vol 116 (3) ◽  
pp. 432-437 ◽  
Author(s):  
Timothy L. Bullock ◽  
G. Parthasarathy ◽  
Karen L. King ◽  
Helen M. Kent ◽  
Thomas M. Roberts ◽  
...  

2005 ◽  
Vol 15 (5) ◽  
pp. R153 ◽  
Author(s):  
Thomas M. Roberts

1989 ◽  
Vol 36 (2) ◽  
pp. 119-126 ◽  
Author(s):  
Alan L. Scott ◽  
Jonathan Dinman ◽  
Daniel J. Sussman ◽  
Pornwadee Yenbutr ◽  
Samuel Ward

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