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Activation and nuclear translocation of ERK1/2 by the formyl peptide receptor is regulated by G protein and is not dependent on beta-arrestin translocation or receptor endocytosis.

eagle-i ID

http://montana.eagle-i.net/i/00000131-0023-5b92-44b9-3efb80000000

Resource Type

  1. Journal article

Properties

  1. Resource Description
    G protein-coupled receptors (GPCRs) transmit diverse cellular signals in response to a large number of stimuli such as chemoattractants, lipids, neurotransmitters, odorants and light. The classical signaling pathway is through heterotrimeric G proteins, but GPCRs can also transmit signals through mechanisms that are not dependent on G proteins. In mammalian cells, the key component for this type of signaling is the family of scaffolding molecules called beta-arrestins. They can function as scaffolds for activation of mitogen-activated protein kinases, including extracellular signal-regulated kinases 1 and 2 (ERK1/2). In this study we examined the role of G protein and beta-arrestin in formyl peptide receptor (FPR)-mediated activation of chemotaxis, receptor endocytosis and ERK1/2 activation using wild type and mutant receptors. Our findings suggest that, unlike certain other GPCRs that can activate ERK1/2 without the involvement of G protein, FPR requires signaling through a G protein-mediated pathway. Previous observations have shown that ERK1/2, activated through G protein, translocates to the nucleus where it stimulates transcription factors. In contrast, the scaffolding protein beta-arrestin retains the activated ERK1/2 in the cytoplasm to allow phosphorylation of cytoplasmic targets. Our experimental data show that both wild-type FPR and a mutant FPR, defective in beta-arrestin binding, induce nuclear translocation of activated ERK1/2 with similar ligand concentration dependence as seen for activation of cytosolic ERK1/2. We propose that FPR-mediated activation of ERK1/2 takes place primarily through G protein and is physiologically important to ensure transcriptional activation of myeloid immunomodulators, such as cytokines.
  2. Website(s)
    http://www.ncbi.nlm.nih.gov/pubmed/16038804
  3. PubMed ID
    16038804
 
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Provenance Metadata About This Resource Record
  1. workflow state
    Published
  2. contributor
    qking (Quinton King)
  3. created
    2011-07-06T10:49:38.296-05:00
  4. creator
    qking (Quinton King)
  5. modified
    2011-07-06T23:28:37.981-05:00

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