7e1t | pdb_00007e1t
Crystal structure of Rab9A-GTP-Nde1
Structural highlights
FunctionRAB9A_HUMAN Involved in the transport of proteins between the endosomes and the trans Golgi network. Publication Abstract from PubMedRab9 is mainly located on late endosomes and required for their intracellular transport to trans-Golgi network (TGN). The cytoplasmic dynein motor, together with its regulatory proteins Nde1/Ndel1 and Lis1, controls intracellular retrograde transport of membranous organelles along the microtubule network. How late endosomes are tethered to the microtubule-based motor dynein for their retrograde transport remains unclear. Here, we demonstrate that the guanosine triphosphate (GTP)-bound Rab9A/B specifically uses Nde1/Ndel1 as an effector to interact with the dynein motor complex. We determined the crystal structure of Rab9A-GTP in complex with the Rab9-binding region of Nde1. The functional roles of key residues involved in the Rab9A-Nde1 interaction are verified using biochemical and cell biology assays. Rab9A mutants unable to bind to Nde1 also failed to associate with dynein, Lis1, and dynactin. Therefore, Nde1 is a Rab9 effector that tethers Rab9-associated late endosomes to the dynein motor for their retrograde transport to the TGN. Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex.,Zhang Y, Chen Z, Wang F, Sun H, Zhu X, Ding J, Zhang T Structure. 2022 Mar 3;30(3):386-395.e5. doi: 10.1016/j.str.2021.10.013. Epub 2021 , Nov 17. PMID:34793709[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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