Receptors for auxin: will it all end in TIRs?

Abstract

The role of TIR1 in ubiquitination and regulated degradation of Aux/IAA transcription factors has been recognized for some years, but recent results have shown that TIR1 itself is also the binding site for auxin. The affinity and specificity of TIR1 match properties anticipated of a nuclear auxin receptor and we look at how they compare with the properties of ABP1. We also consider the mechanism of auxin action via TIR1 and the likelihood that the TIR1 family could account for all auxin responses. It seems likely that the TIR1 system can account for a large part of the repertoire of auxin-mediated responses, but maybe not all.