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Review
. 2008 Aug;147(4):1560-4.
doi: 10.1104/pp.108.120501.

Plasma membrane receptor complexes

José Aker  1 , Sacco C de Vries
Affiliations
Review

Plasma membrane receptor complexes

José Aker et al. Plant Physiol. 2008 Aug.
No abstract available

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Interacting partners in BR signaling. BKI1 binds to the BRI1 homodimer, thus preventing interaction with BAK1/SERK3. Upon binding of brassinolide (BL) to BRI1, BKI1 dissociates from the receptor and dimerization and transphosphorylation take place with SERK1/SERK3 (BAK1). Subsequently phosphorylation of BZR1 by BIN2 is inhibited, and the phosphatase BSU1 is activated. This leads to accumulation of dephosphorylated BZR1 and BES1 in the nucleus, which induces gene transcription. Furthermore, phosphorylated BZR1 translocated to the cytoplasm is retained there by 14-3-3 proteins, and only dephosphorylated BZR1 translocates back to the nucleus.
Figure 2.
Figure 2.
Hypothetical degradation pathways of the SERK1 receptor after activation. Upon binding of the BR brassinolide, BRI1, and SERK1 (and/or SERK3), receptors dimerize and transphosphorylate. After activation, monoubiquitination is a signal for internalization (via clathrin-coated pits?), acquiring the phosphatase KAPP, to give rise to early endosomes. From these endosomes, the receptors can recycle to the PM or are targeted to MVBs and subsequently to lysosomes or vacuoles to be degraded. A, Polyubiquitination after activation of the receptors is a signal for degradation in the proteasome, acquiring adaptor proteins and CDC48A. B, Misfolded SERK1 receptors are pulled out of the ER lumen, polyubiquitinated, and targeted to the proteasome, acquiring CDC48A again.
See this image and copyright information in PMC

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