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Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. / Rodríguez-Concepción, Manuel; Toledo-Ortiz, Gabriela; Yalovsky, Shaul et al.
In: The Plant Journal, Vol. 24, No. 6, 12.2000, p. 775-784.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Rodríguez-Concepción, M, Toledo-Ortiz, G, Yalovsky, S, Caldelari, D & Gruissem, W 2000, 'Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein', The Plant Journal, vol. 24, no. 6, pp. 775-784. https://doi.org/10.1111/j.1365-313X.2000.00924.x

APA

Rodríguez-Concepción, M., Toledo-Ortiz, G., Yalovsky, S., Caldelari, D., & Gruissem, W. (2000). Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. The Plant Journal, 24(6), 775-784. https://doi.org/10.1111/j.1365-313X.2000.00924.x

Vancouver

Rodríguez-Concepción M, Toledo-Ortiz G, Yalovsky S, Caldelari D, Gruissem W. Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. The Plant Journal. 2000 Dec;24(6):775-784. doi: 10.1111/j.1365-313X.2000.00924.x

Author

Rodríguez-Concepción, Manuel ; Toledo-Ortiz, Gabriela ; Yalovsky, Shaul et al. / Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. In: The Plant Journal. 2000 ; Vol. 24, No. 6. pp. 775-784.

Bibtex

@article{ec9d55fdf09a4fa29f313ba39fdf78e1,
title = "Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein",
abstract = "Prenylation is necessary for association of the petunia calmodulin CaM53 with the plasma membrane. To determine whether post-prenylation processing of the protein was also required for plasma membrane targeting, we studied the subcellular localization of a GFP-labelled CaM53 reporter in yeast and plant cells. Blocking of carboxyl-methylation of prenylated proteins either by a specific inhibitor or in mutant yeast cells resulted in localization of green fluorescence to what appears to be the endomembrane system, in contrast with the plasma membrane localization observed in control cells. We show that a prenyl-cysteine methyltransferase (PCM) activity that carboxyl-methylates prenylated CaM53 also exists in plant cells, and that it is required for efficient plasma membrane targeting. We also report an Arabidopsis gene with homology to PCM and demonstrate that it encodes a protein with PCM activity that localizes to the endomembrane system of plant cells, similar to prenylated but unmethylated CaM53. Together, our data suggest that, following prenylation, CaM53 is probably associated with the endomembrane system, where a PCM activity methylates the prenylated protein prior to targeting it to its final destination in the plasma membrane.",
keywords = "Acetylcysteine, Amino Acid Sequence, Animals, Arabidopsis, Calmodulin, Cell Membrane, Cloning, Molecular, Enzyme Inhibitors, Genes, Plant, Humans, Membrane Proteins, Methylation, Methyltransferases, Molecular Sequence Data, Protein Transport, Recombinant Fusion Proteins, Sequence Homology, Solanaceae",
author = "Manuel Rodr{\'i}guez-Concepci{\'o}n and Gabriela Toledo-Ortiz and Shaul Yalovsky and Daniela Caldelari and Wilhelm Gruissem",
year = "2000",
month = dec,
doi = "10.1111/j.1365-313X.2000.00924.x",
language = "English",
volume = "24",
pages = "775--784",
journal = "The Plant Journal",
issn = "0960-7412",
publisher = "Blackwell Publishing Ltd",
number = "6",

}

RIS

TY - JOUR

T1 - Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein

AU - Rodríguez-Concepción, Manuel

AU - Toledo-Ortiz, Gabriela

AU - Yalovsky, Shaul

AU - Caldelari, Daniela

AU - Gruissem, Wilhelm

PY - 2000/12

Y1 - 2000/12

N2 - Prenylation is necessary for association of the petunia calmodulin CaM53 with the plasma membrane. To determine whether post-prenylation processing of the protein was also required for plasma membrane targeting, we studied the subcellular localization of a GFP-labelled CaM53 reporter in yeast and plant cells. Blocking of carboxyl-methylation of prenylated proteins either by a specific inhibitor or in mutant yeast cells resulted in localization of green fluorescence to what appears to be the endomembrane system, in contrast with the plasma membrane localization observed in control cells. We show that a prenyl-cysteine methyltransferase (PCM) activity that carboxyl-methylates prenylated CaM53 also exists in plant cells, and that it is required for efficient plasma membrane targeting. We also report an Arabidopsis gene with homology to PCM and demonstrate that it encodes a protein with PCM activity that localizes to the endomembrane system of plant cells, similar to prenylated but unmethylated CaM53. Together, our data suggest that, following prenylation, CaM53 is probably associated with the endomembrane system, where a PCM activity methylates the prenylated protein prior to targeting it to its final destination in the plasma membrane.

AB - Prenylation is necessary for association of the petunia calmodulin CaM53 with the plasma membrane. To determine whether post-prenylation processing of the protein was also required for plasma membrane targeting, we studied the subcellular localization of a GFP-labelled CaM53 reporter in yeast and plant cells. Blocking of carboxyl-methylation of prenylated proteins either by a specific inhibitor or in mutant yeast cells resulted in localization of green fluorescence to what appears to be the endomembrane system, in contrast with the plasma membrane localization observed in control cells. We show that a prenyl-cysteine methyltransferase (PCM) activity that carboxyl-methylates prenylated CaM53 also exists in plant cells, and that it is required for efficient plasma membrane targeting. We also report an Arabidopsis gene with homology to PCM and demonstrate that it encodes a protein with PCM activity that localizes to the endomembrane system of plant cells, similar to prenylated but unmethylated CaM53. Together, our data suggest that, following prenylation, CaM53 is probably associated with the endomembrane system, where a PCM activity methylates the prenylated protein prior to targeting it to its final destination in the plasma membrane.

KW - Acetylcysteine

KW - Amino Acid Sequence

KW - Animals

KW - Arabidopsis

KW - Calmodulin

KW - Cell Membrane

KW - Cloning, Molecular

KW - Enzyme Inhibitors

KW - Genes, Plant

KW - Humans

KW - Membrane Proteins

KW - Methylation

KW - Methyltransferases

KW - Molecular Sequence Data

KW - Protein Transport

KW - Recombinant Fusion Proteins

KW - Sequence Homology

KW - Solanaceae

U2 - 10.1111/j.1365-313X.2000.00924.x

DO - 10.1111/j.1365-313X.2000.00924.x

M3 - Journal article

C2 - 11135111

VL - 24

SP - 775

EP - 784

JO - The Plant Journal

JF - The Plant Journal

SN - 0960-7412

IS - 6

ER -