beta-Arrestin 1 is required for PAC1 receptor-mediated potentiation of long-lasting ERK1/2 activation by glucose in pancreatic beta-cells

J Biol Chem. 2009 Feb 13;284(7):4332-42. doi: 10.1074/jbc.M807595200. Epub 2008 Dec 11.

Abstract

In pancreatic beta-cells, the pituitary adenylate cyclase-activating polypeptide (PACAP) exerts a potent insulin secretory effect via PAC(1) and VPAC receptors (Rs) through the Galpha(s)/cAMP/protein kinase A pathway. Here, we investigated the mechanisms linking PAC(1)R to ERK1/2 activation in INS-1E beta-cells and pancreatic islets. PACAP caused a transient (5 min) increase in ERK1/2 phosphorylation via PAC(1)Rs and promoted nuclear translocation of a fraction of cytosolic p-ERK1/2. Both protein kinase A- and Src-dependent pathways mediated this transient ERK1/2 activation. Moreover, PACAP potentiated glucose-induced long-lasting ERK1/2 activation. Blocking Ca(2+) influx abolished glucose-induced ERK1/2 activation and PACAP potentiating effect. Glucose stimulation during KCl depolarization showed that, in addition to the triggering signal (rise in cytosolic [Ca(2+)]), the amplifying pathway was also involved in glucose-induced sustained ERK1/2 activation and was required for PACAP potentiation. The finding that at 30 min glucose-induced p-ERK1/2 was detected in both cytosol and nucleus while the potentiating effect of PACAP was only observed in the cytosol, suggested the involvement of the scaffold protein beta-arrestin. Indeed, beta-arrestin 1 (beta-arr1) depletion (in beta-arr1 knockout mouse islets or in INS-1E cells by siRNA) completely abolished PACAP potentiation of long-lasting ERK1/2 activation by glucose. Finally, PACAP potentiated glucose-induced CREB transcriptional activity and IRS-2 mRNA expression mainly via the ERK1/2 signaling pathway, and likewise, beta-arr1 depletion reduced the PACAP potentiating effect on IRS-2 expression. These results establish for the first time that PACAP potentiates glucose-induced long-lasting ERK1/2 activation via a beta-arr1-dependent pathway and thus provide new insights concerning the mechanisms of PACAP and glucose actions in pancreatic beta-cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arrestins / genetics
  • Arrestins / metabolism*
  • Calcium / metabolism
  • Calcium Signaling / drug effects
  • Calcium Signaling / physiology
  • Cell Line
  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism
  • Cyclic AMP Response Element-Binding Protein / genetics
  • Cyclic AMP Response Element-Binding Protein / metabolism
  • Cytosol / metabolism
  • Enzyme Activation / drug effects
  • Enzyme Activation / physiology
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology
  • Glucose / metabolism
  • Glucose / pharmacology*
  • Insulin Receptor Substrate Proteins / biosynthesis
  • Insulin Receptor Substrate Proteins / genetics
  • Insulin-Secreting Cells / cytology
  • Insulin-Secreting Cells / metabolism*
  • MAP Kinase Signaling System / drug effects
  • MAP Kinase Signaling System / physiology
  • Male
  • Mice
  • Mice, Knockout
  • Mitogen-Activated Protein Kinase 1 / genetics
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Mitogen-Activated Protein Kinase 3 / genetics
  • Mitogen-Activated Protein Kinase 3 / metabolism*
  • Phosphorylation / drug effects
  • Phosphorylation / physiology
  • Pituitary Adenylate Cyclase-Activating Polypeptide / genetics
  • Pituitary Adenylate Cyclase-Activating Polypeptide / metabolism
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / genetics
  • Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I / genetics
  • Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I / metabolism*
  • Sweetening Agents / metabolism
  • Sweetening Agents / pharmacology*
  • Time Factors
  • beta-Arrestin 1
  • beta-Arrestins

Substances

  • Adcyap1 protein, mouse
  • Adcyap1r1 protein, mouse
  • Arrb1 protein, mouse
  • Arrestins
  • Creb1 protein, mouse
  • Cyclic AMP Response Element-Binding Protein
  • Insulin Receptor Substrate Proteins
  • Irs2 protein, mouse
  • Pituitary Adenylate Cyclase-Activating Polypeptide
  • RNA, Messenger
  • Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I
  • Sweetening Agents
  • beta-Arrestin 1
  • beta-Arrestins
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Glucose
  • Calcium