Cover Page The handle

In view of the established role of the BTB and TAZ domains in protein-protein interaction, this result suggests that PID interacts with the BTB/POZ domain, and that PBP2 indeed

Aux/IAA proteins are generally short lived, and all gain-of- function mutations in the Aux/ I AA genes led to specific amino acid changes in domain II that stabilize

Previously, a calmodulin, two fsh/Ring class transcription factors and CULLIN3 have been reported as interactors of PBP2 (20, 21). Curiously, none of these proteins

Previously, we showed that PID interacts with the BTB domain containing portion of PBP2 (Figure 1, Chapter 2), and our current finding suggests that PBP2 may act as a scaffold

The NetPhos (Blom et al., 1999) predicted putative phosphorylation sites are boxed and the short version of the PIN1 cytoplasmic loop (PIN1CLsv) used in the in vitro protein

In this chapter we do not only provide data on a possible role of PID as CSN-associated kinase, but our results also suggest that PID reduces IAA12/BDL activity by

(A) Protonated (non- charged) auxin enters the cell by passive diffusion or by active carrier-mediated uptake and induces expression of auxin responsive genes, such

We propose a model that includes PID-dependent PIN phosphorylation at the plasma membrane and the subsequent sorting of PIN proteins to a GNOM-independent pathway for