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

PRA isoforms are targeted to distinct membrane compartments.

M Abdul-Ghani1, P Y Gougeon, D C Prosser

  • 1Loeb Health Research Institute, University of Ottawa, 725 Parkdale Avenue, Ottawa, Ontario, K1Y 4E9 Canada.

The Journal of Biological Chemistry
|November 30, 2000
PubMed
Summary

Prenylated Rab acceptor (PRA) 1 and a newly identified PRA2 isoform bind Rab GTPases. Distinct COOH-terminal motifs dictate their specific localization to the Golgi and endoplasmic reticulum, respectively.

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

Insulin Secretion Predicts the Response to Antidiabetic Therapy in Patients With New-onset Diabetes.

The Journal of clinical endocrinology and metabolism·2021
Same author

Effects of different metabolic states and surgical models on glucose metabolism and secretion of ileal L-cell peptides: results from the HIPER-1 study.

Diabetic medicine : a journal of the British Diabetic Association·2019
Same author

Impact of ethnicity and obesity on insulin resistance in two ethnic groups at very high risk of type 2 diabetes.

Diabetes & metabolism·2016
Same author

Revitalization of pioglitazone: the optimum agent to be combined with a sodium-glucose co-transporter-2 inhibitor.

Diabetes, obesity & metabolism·2016
Same author

Empagliflozin and linagliptin combination therapy for treatment of patients with type 2 diabetes mellitus.

Expert opinion on pharmacotherapy·2015
Same author

Relationship between patient satisfactions with diabetes care and treatment.

Nigerian journal of clinical practice·2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Prenylated Rab acceptor (PRA) 1 binds prenylated Rab GTPases, inhibiting GDI-mediated membrane removal.
  • Rab GTPases are key regulators of intracellular membrane trafficking.

Purpose of the Study:

  • To isolate and characterize a second PRA isoform.
  • To investigate the intracellular localization and sorting mechanisms of PRA isoforms.

Main Methods:

  • Protein isolation and characterization.
  • Immunofluorescence microscopy for intracellular localization studies.
  • Site-directed mutagenesis to map localization signals.

Main Results:

  • A second PRA isoform (PRA2) was identified, binding Rab GTPases independently of guanine nucleotide binding.

Related Experiment Videos

  • PRA1 localizes to the Golgi complex, while PRA2 is found in the endoplasmic reticulum (ER).
  • COOH-terminal DXEE and di-acidic motifs mediate Golgi and ER localization, respectively, for PRA isoforms.

    • Conclusions:

    • Differential intracellular localization of PRA isoforms is determined by distinct COOH-terminal sorting signals.
    • These signals ensure the specific targeting of PRA proteins to the Golgi and ER compartments.
    • Understanding PRA localization is crucial for deciphering Rab GTPase regulation in membrane trafficking.