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- W2023277572 abstract "Mart Saarma has insightfully pointed out many important questions remaining in our understanding of the biological activities and mechanisms of action of glial cell line-derived neurotrophic factor (GDNF) and its receptors. Two of them might already have an answer. The inability of a transmembrane form of GFRα1 [glycosyl phosphatidylinositol (GPI)-anchored co-receptors] to recruit c-Ret to lipid rafts in spite of promoting c-Ret activation is in fact not too surprising, given that the transmembrane domain used in the work alluded to by Saarma was actually taken from a protein that is not normally present in lipid rafts, thereby effectively preventing the mobilization of activated c-Ret to this compartment. Much more interesting would have been to use a transmembrane domain with affinity for lipid rafts, such as one of the hemagglutinin proteins from influenza virus. Regarding the membrane compartmentalization of the constitutively active MEN2A Ret oncogene, our own studies indicate that the majority of this protein is not present in lipid rafts at steady state in fibroblast cells, indicating that the bulk of the signaling by this oncogene occurs outside this compartment. This is in agreement with our observations indicating a transient association of c-Ret with lipid rafts upon activation in cis or in trans. The fate of the c-Ret molecules that exit the rafts after activation and recruitment is unknown, but could conceivably include non-raft portions of the plasma membrane or intracellular compartments, which are also the probable sites of residence of constitutively active MEN2A Ret molecules at steady state." @default.
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- W2023277572 date "2001-08-01" @default.
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- W2023277572 title "Response: GDNF recruits the signaling crew into lipid rafts" @default.
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- W2023277572 doi "https://doi.org/10.1016/s0166-2236(00)01865-8" @default.
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