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  Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3 and Rabin8 effectors to Rab11

Vetter, M., Stehle, R., Basquin, C., & Lorentzen, E. (2015). Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3 and Rabin8 effectors to Rab11. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 22(9), 695-702. doi:10.1038/nsmb.3065.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-95BA-C Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-95BB-A
Genre: Zeitschriftenartikel

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 Urheber:
Vetter, Melanie1, Autor           
Stehle, Ralf2, Autor
Basquin, Claire3, Autor           
Lorentzen, Esben1, Autor           
Affiliations:
1Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565157              
2external, ou_persistent22              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Schlagwörter: POST-GOLGI MEMBRANES; RECYCLING ENDOSOME; PRIMARY CILIOGENESIS; CILIARY MEMBRANE; EXCHANGE FACTOR; TRAFFICKING; ARF; PROTEINS; RHODOPSIN; RECEPTOR
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2015
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000360933200012
DOI: 10.1038/nsmb.3065
 Art des Abschluß: -

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Titel: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 22 (9) Artikelnummer: - Start- / Endseite: 695 - 702 Identifikator: ISSN: 1545-9993