Niemeyer, Michael ORCID: 0000-0001-7501-8879, Castillo, Elena Moreno, Ihling, Christian H., Iacobucci, Claudio ORCID: 0000-0001-9592-3606, Wilde, Verona, Hellmuth, Antje, Hoehenwarter, Wolfgang, Samodelov, Sophia L., Zurbriggen, Matias D. ORCID: 0000-0002-3523-2907, Kastritis, Panagiotis L., Sinz, Andrea and Villalobos, Luz Irina A. Calderon (2020). Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies. Nat. Commun., 11 (1). LONDON: NATURE PUBLISHING GROUP. ISSN 2041-1723

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Abstract

Cullin RING-type E3 ubiquitin ligases SCFTIR1/AFB1-5 and their AUX/IAA targets perceive the phytohormone auxin. The F-box protein TIR1 binds a surface-exposed degron in AUX/IAAs promoting their ubiquitylation and rapid auxin-regulated proteasomal degradation. Here, by adopting biochemical, structural proteomics and in vivo approaches we unveil how flexibility in AUX/IAAs and regions in TIR1 affect their conformational ensemble allowing surface accessibility of degrons. We resolve TIR1.auxin.IAA7 and TIR1.auxin.IAA12 complex topology, and show that flexible intrinsically disordered regions (IDRs) in the degron's vicinity, cooperatively position AUX/IAAs on TIR1. We identify essential residues at the TIR1 N- and C-termini, which provide non-native interaction interfaces with IDRs and the folded PB1 domain of AUX/IAAs. We thereby establish a role for IDRs in modulating auxin receptor assemblies. By securing AUX/IAAs on two opposite surfaces of TIR1, IDR diversity supports locally tailored positioning for targeted ubiquitylation, and might provide conformational flexibility for a multiplicity of functional states. Auxin-mediated recruitment of AUX/IAAs by the F-box protein TIR1 prompts rapid AUX/IAA ubiquitylation and degradation. By resolving auxin receptor topology, the authors show that intrinsically disordered regions near the degrons of two Aux/IAA proteins reinforce complex assembly and position Aux/IAAs for ubiquitylation.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Niemeyer, MichaelUNSPECIFIEDorcid.org/0000-0001-7501-8879UNSPECIFIED
Castillo, Elena MorenoUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Ihling, Christian H.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Iacobucci, ClaudioUNSPECIFIEDorcid.org/0000-0001-9592-3606UNSPECIFIED
Wilde, VeronaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Hellmuth, AntjeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Hoehenwarter, WolfgangUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Samodelov, Sophia L.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Zurbriggen, Matias D.UNSPECIFIEDorcid.org/0000-0002-3523-2907UNSPECIFIED
Kastritis, Panagiotis L.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Sinz, AndreaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Villalobos, Luz Irina A. CalderonUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-334178
DOI: 10.1038/s41467-020-16147-2
Journal or Publication Title: Nat. Commun.
Volume: 11
Number: 1
Date: 2020
Publisher: NATURE PUBLISHING GROUP
Place of Publication: LONDON
ISSN: 2041-1723
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
MOLECULAR-DYNAMICS; TRANSCRIPTION FACTORS; STRUCTURAL BASIS; WEB SERVER; DEGRADATION; UBIQUITIN; MECHANISM; REGIONS; FAMILY; HADDOCKMultiple languages
Multidisciplinary SciencesMultiple languages
URI: http://kups.ub.uni-koeln.de/id/eprint/33417

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