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Ensured auxin sensing by degron flexibility

ABSTRACT: Using a structural proteomics approach via chemical cross-linking combined with mass spectrometry (XL-MS), we have resolved SCFTIR auxin·AUX/IAA complex overall topology, and established the power of IDRs modulating auxin receptor assemblies.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Michael Niemeyer

LAB HEAD: Luz Irina Calderón Villalobos

PROVIDER: PXD015285 | Pride | 2020-05-11

REPOSITORIES: Pride

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Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies.

Niemeyer Michael M Moreno Castillo Elena E Ihling Christian H CH Iacobucci Claudio C Wilde Verona V Hellmuth Antje A Hoehenwarter Wolfgang W Samodelov Sophia L SL Zurbriggen Matias D MD Kastritis Panagiotis L PL Sinz Andrea A Calderón Villalobos Luz Irina A LIA

Nature communications 20200508 1

Cullin RING-type E3 ubiquitin ligases SCF<sup>TIR1/AFB1-5</sup> 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 ...[more]

PMID: 32385295

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