The prenylation status of a novel plant calmodulin directs plasma membrane or nuclear localization of the protein

Manuel Rodríguez-Concepción, Shaul Yalovsky, Moriyah Zik, Hillel Fromm, Wilhelm Gruissem

Research output: Contribution to journalArticlepeer-review

128 Scopus citations

Abstract

Post-translational attachment of isoprenyl groups to conserved cysteine residues at the C-terminus of a number of regulatory proteins is important for their function and subcellular localization. We have identified a novel calmodulin, CaM53, with an extended C-terminal basic domain and a CTIL CaaX-box motif which are required for efficient prenylation of the protein in vitro and in vivo. Ectopic expression of wildtype CaM53 or a non-prenylated mutant protein in plants causes distinct morphological changes. Prenylated CaM53 associates with the plasma membrane, but the non-prenylated mutant protein localizes to the nucleus, indicating a dual role for the C-terminal domain. The subcellular localization of CaM53 can be altered by a block in isoprenoid biosynthesis or sugar depletion, suggesting that CaM53 activates different targets in response to metabolic changes. Thus, prenylation of CaM53 appears to be a novel mechanism by which plant cells can coordinate Ca2+ signaling with changes in metabolic activities.

Original languageEnglish
Pages (from-to)1996-2007
Number of pages12
JournalEMBO Journal
Volume18
Issue number7
DOIs
StatePublished - 1 Apr 1999
Externally publishedYes

Keywords

  • Calmodulin
  • Isoprenoid
  • Membrane
  • Nucleus
  • Prenylation

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