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Characterization of the GbpD-activated Rap1 pathway regulating adhesion and cell polarity in Dictyostelium discoideum

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dc.creator Kortholt, Arjan
dc.creator Van Haastert, Peter J. M.
dc.creator Weeks, Gerald
dc.creator Wittinghofer, Alfred
dc.creator Rehmann, Holger
dc.creator Keizer-Gunnink, Ineke
dc.creator Bosgraaf, Leonard
dc.creator Kae, Helmut
dc.date 2006-08-01T00:00:00Z
dc.date.accessioned 2023-01-09T12:03:43Z
dc.date.available 2023-01-09T12:03:43Z
dc.identifier 69962ac2-18b3-49eb-997a-bb4ed9588d8d
dc.identifier 10.1074/jbc.m600804200
dc.identifier https://avesis.sdu.edu.tr/publication/details/69962ac2-18b3-49eb-997a-bb4ed9588d8d/oai
dc.identifier.uri http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/97955
dc.description The regulation of cell polarity plays an important role in chemotaxis. GbpD, a putative nucleotide exchange factor for small G-proteins of the Ras family, has been implicated in adhesion, cell polarity, and chemotaxis in Dictyostelium. Cells overexpressing GbpD are flat, exhibit strongly increased cell-substrate attachment, and extend many bifurcated and lateral pseudopodia. These cells overexpressing GbpD are severely impaired in chemotaxis, most likely due to the induction of many protrusions rather than an enhanced adhesion. The GbpD-overexpression phenotype is similar to that of cells overexpressing Rap1. Here we demonstrate that GbpD activates Rap1 both in vivo and in vitro but not any of the five other characterized Ras proteins. In a screen for Rap1 effectors, we overexpressed GbpD in several mutants defective in adhesion or cell polarity and identified Phg2 as Rap1 effector necessary for adhesion, but not cell polarity. Phg2, a serine/threonine-specific kinase, directly interacts with Rap1 via its Ras association domain.
dc.language eng
dc.rights info:eu-repo/semantics/openAccess
dc.title Characterization of the GbpD-activated Rap1 pathway regulating adhesion and cell polarity in Dictyostelium discoideum
dc.type info:eu-repo/semantics/article


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