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• W2063710108 abstract "Background RAF kinases direct ERK MAPK signaling to distinct subcellular compartments in response to growth factor stimulation. Methodology/Principal Findings Of the three mammalian isoforms A-RAF is special in that one of its two lipid binding domains mediates a unique pattern of membrane localization. Specific membrane binding is retained by an N-terminal fragment (AR149) that corresponds to a naturally occurring splice variant termed DA-RAF2. AR149 colocalizes with ARF6 on tubular endosomes and has a dominant negative effect on endocytic trafficking. Moreover actin polymerization of yeast and mammalian cells is abolished. AR149/DA-RAF2 does not affect the internalization step of endocytosis, but trafficking to the recycling compartment. Conclusions/Significance A-RAF induced ERK activation is required for this step by activating ARF6, as A-RAF depletion or inhibition of the A-RAF controlled MEK-ERK cascade blocks recycling. These data led to a new model for A-RAF function in endocytic trafficking." @default.
• W2063710108 created "2016-06-24" @default.
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• W2063710108 date "2009-02-27" @default.
• W2063710108 modified "2023-09-26" @default.
• W2063710108 title "A-RAF Kinase Functions in ARF6 Regulated Endocytic Membrane Traffic" @default.
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• W2063710108 doi "https://doi.org/10.1371/journal.pone.0004647" @default.
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