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PMID:21864294

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Citation

Pribat, A, Sormani, R, Rousseau-Gueutin, M, Julkowska, MM, Testerink, C, Joubès, J, Castroviejo, M, Laguerre, M, Meyer, C, Germain, V and Rothan, C (2012) A novel class of PTEN protein in Arabidopsis displays unusual phosphoinositide phosphatase activity and efficiently binds phosphatidic acid. Biochem. J. 441:161-71

Abstract

PTEN (phosphatase and tensin homologue deleted on chromosome ten) proteins are dual phosphatases with both protein and phosphoinositide phosphatase activity. They modulate signalling pathways controlling growth, metabolism and apoptosis in animals and are implied in several human diseases. In the present paper we describe a novel class of PTEN pro-teins in plants, termed PTEN2, which comprises the AtPTEN (Arabidopsis PTEN) 2a and AtPTEN2b proteins in Arabidopsis. Both display low in vitro tyrosine phosphatase activity. In addition, AtPTEN2a actively dephosphorylates in vitro the 3' phosphate group of PI3P (phosphatidylinositol 3-phosphate), PI(3,4)P2 (phosphatidylinositol 3,4-bisphosphate) and PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate). In contrast with animal PTENs, PI(3,4,5)P3 (phosphatidylinositol 3,4,5-trisphosphate) is a poor substrate. Site-directed mutagenesis of AtPTEN2a and molecular modelling of protein-phosphoinositide interactions indicated that substitutions at the PTEN2 core catalytic site of the Lys267 and Gly268 residues found in animals, which are critical for animal PTEN activity, by Met267 and Ala268 found in the eudicot PTEN2 are responsible for changes in substrate specificity. Remarkably, the AtPTEN2a protein also displays strong binding activity for PA (phosphatidic acid), a major lipid second messenger in plants. Promoter::GUS (β-glucuronidase) fusion, transcript and protein analyses further showed the transcriptional regulation of the ubiquitously expressed AtPTEN2a and AtPTEN2b by salt and osmotic stress. The results of the present study suggest a function for this novel class of plant PTEN proteins as an effector of lipid signalling in plants.

Links

PubMed Online version:10.1042/BJ20110776

Keywords

Arabidopsis/genetics; Arabidopsis/metabolism; Arabidopsis Proteins/genetics; Arabidopsis Proteins/metabolism; Escherichia coli/metabolism; Gene Expression Regulation, Plant/physiology; Models, Molecular; PTEN Phosphohydrolase/genetics; PTEN Phosphohydrolase/metabolism; Phosphatidic Acids/metabolism; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Phylogeny; Protein Binding; Protein Conformation; Signal Transduction; Substrate Specificity

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ARATH:PTN2B

involved_in

GO:0006970: response to osmotic stress

ECO:0000270: expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:PTN2B

involved_in

GO:0009651: response to salt stress

ECO:0000270: expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:PTN2B

enables

GO:0052866: phosphatidylinositol phosphate phosphatase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ARATH:PTN2A

involved_in

GO:0006970: response to osmotic stress

ECO:0000270: expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:PTN2A

involved_in

GO:0009651: response to salt stress

ECO:0000270: expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:PTN2A

enables

GO:0004725: protein tyrosine phosphatase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ARATH:PTN2A

acts_upstream_of_or_within

GO:0046856: phosphatidylinositol dephosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:PTN2A

enables

GO:0052866: phosphatidylinositol phosphate phosphatase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ARATH:PTN2A

enables

GO:0070300: phosphatidic acid binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ARATH:PTN2A

acts_upstream_of_or_within

GO:0035335: peptidyl-tyrosine dephosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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