A-RAF kinase functions in ARF6 regulated endocytic membrane traffic.
<h4>Background</h4>RAF kinases direct ERK MAPK signaling to distinct subcellular compartments in response to growth factor stimulation.<h4>Methodology/principal findings</h4>Of the three mammalian isoforms A-RAF is special in that one of its two lipid binding domains mediates...
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| Autores principales: | , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Public Library of Science (PLoS)
2009
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/0bdac0f91c3c4d48afbb205d0c60fa7e |
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| Sumario: | <h4>Background</h4>RAF kinases direct ERK MAPK signaling to distinct subcellular compartments in response to growth factor stimulation.<h4>Methodology/principal findings</h4>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.<h4>Conclusions/significance</h4>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. |
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