Residues 762-801 of PLD1 mediate the interaction with PED/PEA15 (475 views)
Mol Biosyst (ISSN: 1742-206x), 2010 Oct; 6(10): 2039-2048.
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Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77956522887&partnerID=40&md5=eca30cf85825325adc033ad504d7c666
Keywords: Pea15 Protein, Human, Phospholipase D, Phosphoprotein, Primer Dna, Signal Peptide, Article, Chemistry, Metabolism, Nucleotide Sequence, Protein Binding, Signal Transduction, Site Directed Mutagenesis, Base Sequence, Dna Primers, Intracellular Signaling Peptides And Proteins, Site-Directed, Animalia,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini (IBB), CNR, via Mezzocannone 16, 80134, Napoli, Italy
Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università di Napoli Federico II, Napoli, Italy
Dipartimento Delle Scienze Biologiche, Università di Napoli Federico II, via Mezzocannone 16, 80134, Napoli, Italy
Istituto di Endocrinologia e Oncologia Sperimentale Gaetano Salvatore, Consiglio Nazionale Delle Ricerche, Napoli, Italy
References:
Not available.
Mol Biosyst (ISSN: 1742-206x), 2010 Oct; 6(10): 2039-2048.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77956522887&partnerID=40&md5=eca30cf85825325adc033ad504d7c666
Keywords: Pea15 Protein, Human, Phospholipase D, Phosphoprotein, Primer Dna, Signal Peptide, Article, Chemistry, Metabolism, Nucleotide Sequence, Protein Binding, Signal Transduction, Site Directed Mutagenesis, Base Sequence, Dna Primers, Intracellular Signaling Peptides And Proteins, Site-Directed, Animalia,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini (IBB), CNR, via Mezzocannone 16, 80134, Napoli, Italy
Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università di Napoli Federico II, Napoli, Italy
Dipartimento Delle Scienze Biologiche, Università di Napoli Federico II, via Mezzocannone 16, 80134, Napoli, Italy
Istituto di Endocrinologia e Oncologia Sperimentale Gaetano Salvatore, Consiglio Nazionale Delle Ricerche, Napoli, Italy
References:
Not available.
Residues 762-801 of PLD1 mediate the interaction with PED/PEA15
The interaction of Phospholipase D1 (PLD1) by its C-terminal domain D4 with PED/PEA15 has been indicated as a target for type 2 diabetes. PED/PEA15 is overexpressed in several tissues of individuals affected by type 2 diabetes and its overexpression in intact cells and in transgenic animal models impairs insulin regulation of glucose transport by a mechanism mediated by the interaction with D4 and the consequent increase of protein kinase C-α activity. Expression of D4 or administration of a peptide mimicking the PED/PEA15 region involved in this interaction to cells stably overexpressing PED/PEA15 reduces its interaction with PLD1, thereby lowering PKC-α activation and restoring normal glucose transport mediated by PKC-ζ. By using D4 deletion mutants, we have restricted the PLD1 region involved in PED/PEA15 interaction to an N-terminal fragment named D4α (residues 712-818). This region binds PED/PEA15 with the same efficacy as D4 (K D ∼ 0.7 μM) and, when transfected in different PED/PEA15-overexpressing cells, it is able to reduce PKC-α activity and to restore the sensitivity of PKC-ζ to insulin stimulation, independently of the PI3K/Akt signalling. We also show that the effective disruption of the PED/PEA15-PLD1 interaction can restore the normal ERK1/2 signalling. Finally, using a set of overlapping peptides that cover the D4α region, we have further restricted the shortest PED/PEA15-binding site to a segment encompassing residues 762-801, suggesting that a quite limited binding interface mostly contributes to the interaction and can thus be a selective target for the design of effective antagonists. © 2010 The Royal Society of Chemistry.
The interaction of Phospholipase D1 (PLD1) by its C-terminal domain D4 with PED/PEA15 has been indicated as a target for type 2 diabetes. PED/PEA15 is overexpressed in several tissues of individuals affected by type 2 diabetes and its overexpression in intact cells and in transgenic animal models impairs insulin regulation of glucose transport by a mechanism mediated by the interaction with D4 and the consequent increase of protein kinase C-α activity. Expression of D4 or administration of a peptide mimicking the PED/PEA15 region involved in this interaction to cells stably overexpressing PED/PEA15 reduces its interaction with PLD1, thereby lowering PKC-α activation and restoring normal glucose transport mediated by PKC-ζ. By using D4 deletion mutants, we have restricted the PLD1 region involved in PED/PEA15 interaction to an N-terminal fragment named D4α (residues 712-818). This region binds PED/PEA15 with the same efficacy as D4 (K D ∼ 0.7 μM) and, when transfected in different PED/PEA15-overexpressing cells, it is able to reduce PKC-α activity and to restore the sensitivity of PKC-ζ to insulin stimulation, independently of the PI3K/Akt signalling. We also show that the effective disruption of the PED/PEA15-PLD1 interaction can restore the normal ERK1/2 signalling. Finally, using a set of overlapping peptides that cover the D4α region, we have further restricted the shortest PED/PEA15-binding site to a segment encompassing residues 762-801, suggesting that a quite limited binding interface mostly contributes to the interaction and can thus be a selective target for the design of effective antagonists. © 2010 The Royal Society of Chemistry.
Residues 762-801 of PLD1 mediate the interaction with PED/PEA15
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Residues 762-801 of PLD1 mediate the interaction with PED/PEA15
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14 Records (12 excluding Abstracts).
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Total 5 year impact factor: 56.473 (43.582 excluding Abstracts).
Total impact factor: 58.321 (45.389 excluding Abstracts).
Total 5 year impact factor: 56.473 (43.582 excluding Abstracts).
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