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Ponticulin plays a role in the positional stabilization of pseudopods.
J Cell Biol
December 1995
Department of Biological Sciences, University of Iowa, Iowa City 52242, USA.
Ponticulin is a 17-kD glycoprotein that represents a major high affinity link between the plasma membrane and the cortical actin network of Dictyostelium. To assess the role of ponticulin in pseudopod extension and retraction, the motile behavior of two independently generated mutants lacking ponticulin was analyzed using computer-assisted two- and three-dimensional motion analysis systems. More than half of the lateral pseudopods formed off the substratum by ponticulin-minus cells slipped relative to the substratum during extension and retraction.
View Article and Find Full Text PDFPonticulin is the major high affinity link between the plasma membrane and the cortical actin network in Dictyostelium.
J Cell Biol
September 1994
Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
Interactions between the plasma membrane and underlying actin-based cortex have been implicated in membrane organization and stability, the control of cell shape, and various motile processes. To ascertain the function of high affinity actin-membrane associations, we have disrupted by homologous recombination the gene encoding ponticulin, the major high affinity actin-membrane link in Dictyostelium discoideum amoebae. Cells lacking detectable amounts of ponticulin message and protein also are deficient in high affinity actin-membrane binding by several criteria.
View Article and Find Full Text PDFPonticulin is an atypical membrane protein.
J Cell Biol
September 1994
Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
We have cloned and sequenced ponticulin, a 17,000-dalton integral membrane glycoprotein that binds F-actin and nucleates actin assembly. A single copy gene encodes a developmentally regulated message that is high during growth and early development, but drops precipitously during cell streaming at approximately 8 h of development. The deduced amino acid sequence predicts a protein with a cleaved NH2-terminal signal sequence and a COOH-terminal glycosyl anchor.
View Article and Find Full Text PDFRole of actin polymerization in cell locomotion: molecules and models.
Am J Respir Cell Mol Biol
June 1993
Department of Pathology and Laboratory Medicine, Brown University, Providence, Rhode Island.
Actin filaments forming at the anterior margin of a migrating cell are essential for the formation of filopodia, lamellipodia, and pseudopodia, the "feet" that the cell extends before it. These structures in turn are required for cell locomotion. Yet the molecular nature of the "nucleator" that seeds the polymerization of actin at the leading edge is unknown.
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