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| Meth. Enzymol. (2005); 403:599-607 | |
| Affinity purification of Ypt6 effectors and identification of TMF-ARA160 as a Rab6 interactor- | |
| Siniossoglou S | |
| Abstract: 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- | |
| [PUBMED: 16473623] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |