Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity.

C Chen1, H Wang, C W Fong

  • 1Regulatory Biology Group, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Singapore.

FEBS Letters
|August 28, 2001
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tuberculous tenosynovitis and bursitis: imaging findings in 21 cases.

Radiology·1996
Same author

Recombinant mitotoxin basic fibroblast growth factor-saporin reduces venous anastomotic intimal hyperplasia in the arteriovenous graft.

Circulation·1996
Same author

Measurement of urinary estrogen metabolites using a monoclonal enzyme-linked immunoassay kit: assay performance and feasibility for epidemiological studies.

Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology·1996
Same author

Differences in cholinergic responses from outer hair cells of rat and guinea pig.

Hearing research·1996
Same author

Pharmacokinetics of retinoids in women after meal consumption or vitamin A supplementation.

Journal of clinical pharmacology·1996
Same author

Determination of the amino acid residue involved in [3H]beta-funaltrexamine covalent binding in the cloned rat mu-opioid receptor.

The Journal of biological chemistry·1996

Regulators of G-protein signaling (RGS) proteins are key regulators of cellular communication. This study reveals how phosphorylation of RGS16 by G-protein-coupled receptors inhibits its function, impacting cellular signaling pathways.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Regulators of G-protein signaling (RGS) proteins function as GTPase-activating proteins (GAP) for Galpha subunits.
  • RGS proteins play critical roles in modulating G-protein signaling pathways, which are involved in numerous physiological processes.

Purpose of the Study:

  • To investigate the phosphorylation status and functional consequences of RGS16 in response to G-protein-coupled receptor (GPCR) stimulation.
  • To determine how specific phosphorylation sites on RGS16 affect its GTPase-activating protein (GAP) activity and downstream signaling.

Main Methods:

  • In vivo orthophosphate labeling experiments in HEK293T cells.
  • Expression of mouse RGS16 and the alpha2A adrenergic receptor.
  • Analysis of RGS16 phosphorylation at serine 194 (constitutive) and serine 53 (ligand-dependent).

Related Experiment Videos

  • Assays to measure RGS16 GAP activity and its effect on heterotrimeric G-protein-stimulated extracellular signal-regulated protein kinase (ERK) activity.

    • Main Results:

    • Mouse RGS16 is constitutively phosphorylated at serine 194.
    • Epinephrine stimulation of cells expressing the alpha2A adrenergic receptor induces ligand-dependent phosphorylation of RGS16 at serine 53.
    • Phosphorylation at both serine 194 and serine 53 impairs RGS16's GAP activity.
    • Impaired RGS16 GAP activity leads to reduced attenuation of heterotrimeric G-protein-stimulated ERK activity.

    Conclusions:

    • This study demonstrates, for the first time, the functional downregulation of RGS16 by phosphorylation mediated by a G-protein-coupled receptor.
    • Phosphorylation of RGS16 by GPCRs serves as a mechanism to modulate cellular signaling by inhibiting RGS protein function.
    • These findings provide novel insights into the intricate regulation of G-protein signaling pathways.