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. 1999 Apr 1;18(7):1996–2007. doi: 10.1093/emboj/18.7.1996

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

M Rodríguez-Concepción 1, S Yalovsky 1, M Zik 1, H Fromm 1, W Gruissem 1
PMCID: PMC1171284  PMID: 10202162

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 wild-type 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.

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Selected References

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