8A4A
Structure of human Rep15 in complex with bovine Rab3C.
Summary for 8A4A
| Entry DOI | 10.2210/pdb8a4a/pdb |
| Descriptor | Rab15 effector protein, Ras-related protein Rab-3C, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | rab gtpase, endocytosis |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 53470.78 |
| Authors | Rai, A.,Vetter, I.R.,Goody, R.S. (deposition date: 2022-06-10, release date: 2022-08-10, Last modification date: 2024-01-31) |
| Primary citation | Rai, A.,Singh, A.K.,Bleimling, N.,Posern, G.,Vetter, I.R.,Goody, R.S. Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. Nat Commun, 13:4262-4262, 2022 Cited by PubMed Abstract: In their GTP-bound (active) form, Rab proteins interact with effector proteins that control downstream signaling. One such Rab15 effector is Rep15, which is known to have a role in receptor recycling from the endocytic recycling compartment but otherwise remains poorly characterized. Here, we report the characterization of the Rep15:Rab15 interaction and identification of Rab3 paralogs and Rab34 as Rep15 interacting partners from a yeast two-hybrid assay. Biochemical validation of the interactions is presented and crystal structures of the Rep15:Rab3B and Rep15:Rab3C complexes provide additional mechanistic insight. We find that Rep15 adopts a globular structure that is distinct from other reported Rab15, Rab3 and Rab34 effectors. Structure-based mutagenesis experiments explain the Rep15:Rab interaction specificity. Rep15 depletion in U138MG glioblastoma cells impairs cell proliferation, cell migration and receptor recycling, underscoring the need for further clarification of the role of Rep15 in cancer. PubMed: 35871249DOI: 10.1038/s41467-022-31831-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.52 Å) |
Structure validation
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