ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor

R. Mitchell, D.N. Robertson, P.J. Holland, D. Collins, E.M. Lutz, M.S. Johnson

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

G protein-coupled receptors can potentially activate phospholipase D (PLD) by a number of routes. We show here that the native M3 muscarinic receptor in 1321N1 cells and an epitope-tagged M3 receptor expressed in COS7 cells substantially utilize an ADP-ribosylation factor (ARF)-dependent route of PLD activation. This pathway is activated at the plasma membrane but appears to be largely independent of Gq/11, phospholipase C, Ca2, protein kinase C, tyrosine kinases, and phosphatidyl inositol 3-kinase. We report instead that it involves physical association of ARF with the M3 receptor as demonstrated by co-immunoprecipitation and by in vitro interaction with a glutathione S-transferase fusion protein of the receptor's third intracellular loop domain. Experiments with mutant constructs of ARF1/6 and PLD1/2 indicate that the M3 receptor displays a major ARF1-dependent route of PLD1 activation with an additional ARF6-dependent pathway to PLD1 or PLD2. Examples of other G protein-coupled receptors assessed in comparison display alternative pathways of protein kinase C- or ARF6-dependent activation of PLD2.
LanguageEnglish
Pages33818-33830
Number of pages12
JournalJournal of Biological Chemistry
Volume278
Issue number36
DOIs
Publication statusPublished - 5 Sep 2003

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ADP-Ribosylation Factors
Phospholipase D
Muscarinic Receptors
Chemical activation
Muscarinic M3 Receptors
Phosphatidylinositol 3-Kinase
Type C Phospholipases
G-Protein-Coupled Receptors
Glutathione Transferase
GTP-Binding Proteins
Immunoprecipitation
Protein-Tyrosine Kinases
Epitopes
Phosphotransferases
Cell Membrane
Cell membranes
Protein Kinase C
Display devices
Association reactions
Experiments

Keywords

  • ADP-ribosylation
  • phospholipase D
  • M-3 muscarinic receptor

Cite this

Mitchell, R., Robertson, D. N., Holland, P. J., Collins, D., Lutz, E. M., & Johnson, M. S. (2003). ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor. Journal of Biological Chemistry, 278(36), 33818-33830. https://doi.org/10.1074/jbc.M305825200
Mitchell, R. ; Robertson, D.N. ; Holland, P.J. ; Collins, D. ; Lutz, E.M. ; Johnson, M.S. / ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 36. pp. 33818-33830.
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Mitchell, R, Robertson, DN, Holland, PJ, Collins, D, Lutz, EM & Johnson, MS 2003, 'ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor' Journal of Biological Chemistry, vol. 278, no. 36, pp. 33818-33830. https://doi.org/10.1074/jbc.M305825200

ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor. / Mitchell, R.; Robertson, D.N.; Holland, P.J.; Collins, D.; Lutz, E.M.; Johnson, M.S.

In: Journal of Biological Chemistry, Vol. 278, No. 36, 05.09.2003, p. 33818-33830.

Research output: Contribution to journalArticle

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T1 - ADP-ribosylation factor-dependent phospholipase D activation by the M-3 muscarinic receptor

AU - Mitchell, R.

AU - Robertson, D.N.

AU - Holland, P.J.

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AU - Johnson, M.S.

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N2 - G protein-coupled receptors can potentially activate phospholipase D (PLD) by a number of routes. We show here that the native M3 muscarinic receptor in 1321N1 cells and an epitope-tagged M3 receptor expressed in COS7 cells substantially utilize an ADP-ribosylation factor (ARF)-dependent route of PLD activation. This pathway is activated at the plasma membrane but appears to be largely independent of Gq/11, phospholipase C, Ca2, protein kinase C, tyrosine kinases, and phosphatidyl inositol 3-kinase. We report instead that it involves physical association of ARF with the M3 receptor as demonstrated by co-immunoprecipitation and by in vitro interaction with a glutathione S-transferase fusion protein of the receptor's third intracellular loop domain. Experiments with mutant constructs of ARF1/6 and PLD1/2 indicate that the M3 receptor displays a major ARF1-dependent route of PLD1 activation with an additional ARF6-dependent pathway to PLD1 or PLD2. Examples of other G protein-coupled receptors assessed in comparison display alternative pathways of protein kinase C- or ARF6-dependent activation of PLD2.

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