Affinity purification of Ypt6 effectors and identification of TMF/ARA160 as a Rab6 interactor.
Rab/Ypt GTPases are key regulators of intracellular traffic in eukaryotic cells. One important function of Rab/Ypts is the nucleotide-dependent recruitment of downstream effector molecules onto the membrane of organelles. In budding yeast Ypt6 is required for recycling of membrane proteins from endosomes back to the Golgi. A biochemical approach based on the affinity purification of Ypt6:GTP-interacting proteins from yeast cytosol led to the identification of two conserved Ypt6 effectors, the tetrameric VFT complex and Sgm1. The mammalian homolog of Sgm1, TMF/ARA160, contains a short conserved coiled-coil motif that is sufficient for the binding to the three mammalian orthologs of Ypt6, Rab6A, Rab6A', and Rab6B.
Symeon
S
Siniossoglou
D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism*; D002846:Chromatography, Affinity / Q000379:methods*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D020559:Monomeric GTP-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000302:isolation & purification* / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
D048868:Adaptor Proteins, Signal Transducing; D004268:DNA-Binding Proteins; C094135:Rab6 protein; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C077335:TMF1 protein, human; D020559:Monomeric GTP-Binding Proteins; C499307:YPT6 protein, S cerevisiae; D020691:rab GTP-Binding Proteins