4UJ3

Crystal structure of human Rab11-Rabin8-FIP3

Summary for 4UJ3

• Entry DOI: 10.2210/pdb4uj3/pdb
• Related: 4UJ4 4UJ5
• Descriptor: RAS-RELATED PROTEIN RAB-11A, RAB-3A-INTERACTING PROTEIN, RAB11 FAMILY-INTERACTING PROTEIN 3, ... (8 entities in total)
• Functional Keywords: transport protein, ciliary targeting complex, cilium, vesicular transport, membrane trafficking
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cell membrane; Peripheral membrane protein: P62491; Cytoplasm: Q96QF0; Recycling endosome membrane; Peripheral membrane protein: O75154
• Total number of polymer chains: 24
• Total formula weight: 409489.46

Authors

Vetter, M.,Lorentzen, E. (deposition date: 2015-04-08, release date: 2015-08-12, Last modification date: 2024-01-10)

Primary citation

Vetter, M.,Stehle, R.,Basquin, C.,Lorentzen, E.
Structure of Rab11-Fip3-Rabin8 Reveals Simultaneous Binding of Fip3 and Rabin8 Effectors to Rab11.
Nat.Struct.Mol.Biol., 22:695-, 2015

PubMed Abstract: The small GTPase Rab11 and its effectors FIP3 and Rabin8 are essential to membrane-trafficking pathways required for cytokinesis and ciliogenesis. Although effector binding is generally assumed to be sequential and mutually exclusive, we show that Rab11 can simultaneously bind FIP3 and Rabin8. We determined crystal structures of human Rab11-GMPPNP-Rabin8 and Rab11-GMPPNP-FIP3-Rabin8. The structures reveal that the C-terminal domain of Rabin8 adopts a previously undescribed fold that interacts with Rab11 at an unusual effector-binding site neighboring the canonical FIP3-binding site. We show that Rab11-GMPPNP-FIP3-Rabin8 is more stable than Rab11-GMPPNP-Rabin8, owing to direct interaction between Rabin8 and FIP3 within the dual effector-bound complex. The data allow us to propose a model for how membrane-targeting complexes assemble at the trans-Golgi network and recycling endosomes, through multiple weak interactions that create high-avidity complexes.

PubMed: 26258637
DOI: 10.1038/NSMB.3065

Experimental method

X-RAY DIFFRACTION (3 Å)