The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP

I.M. Rienties, J. Vink, J.W. Borst, E.T. Russinova, S.C. de Vries

Research output: Contribution to journalArticleAcademicpeer-review

46 Citations (Scopus)

Abstract

Leucine-rich repeat (LRR)-containing transmembrane receptor-like kinases (RLKs) are important components of plant signal transduction. The Arabidopsis thaliana somatic embryogenesis receptor-like kinase 1 (AtSERK1) is an LRR-RLK proposed to participate in a signal transduction cascade involved in embryo development. By yeast two-hybrid screening we identified AtCDC48, a homologue of the mammalian AAA-ATPase p97 and GF14, a member of the Arabidopsis family of 14-3-3 proteins as AtSERK1 interactors. In vitro, the AtSERK1 kinase domain is able to transphosphorylate and bind both AtCDC48 and GF14. In yeast, AtCDC48 interacts with GF14 and with the PP2C phosphatase KAPP. In plant protoplasts AtSERK1 interacts with GF14.
Original languageEnglish
Pages (from-to)394-405
JournalPlanta
Volume221
Issue number3
DOIs
Publication statusPublished - 2005

Keywords

  • embryogenesis receptor kinase-1
  • cell-cycle
  • tyrosine phosphorylation
  • signal-transduction
  • membrane-fusion
  • binding
  • cdc48p
  • gene
  • expression
  • homolog

Fingerprint Dive into the research topics of 'The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP'. Together they form a unique fingerprint.

Cite this