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Structural and functional analysis of the GABARAP interaction motif (GIM)
Authors:Diana O Rios‐Szwed  Hironori Suzuki  Andreas Kniss  Frank Löhr  Soichi Wakatsuki  Volker Dötsch  Ivan Dikic  Renwick CJ Dobson  David G McEwan
Institution:1. Division of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK;2. Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand;3. Structural Biology Research Centre, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, Japan;4. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt am Main, Germany;5. Photon Science, SLAC National Accelerator Laboratory, Menlo Park, CA, USA;6. Structural Biology (School of Medicine), Beckman Center B105, Stanford, CA, USA;7. Institute of Biochemistry II, Goethe University School of Medicine, Frankfurt (Main), Germany;8. Buchmann Institute for Molecular Life Sciences, Goethe University, Frankfurt am Main, Germany;9. Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne, Parkville, Vic., Australia
Abstract:Through the canonical LC3 interaction motif (LIR), W/F/Y]‐X1‐X2‐I/L/V], protein complexes are recruited to autophagosomes to perform their functions as either autophagy adaptors or receptors. How these adaptors/receptors selectively interact with either LC3 or GABARAP families remains unclear. Herein, we determine the range of selectivity of 30 known core LIR motifs towards individual LC3s and GABARAPs. From these, we define a I nteraction
Keywords:autophagy  Atg8  GABARAP  LC3  PLEKHM1
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