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

Assaying phosphoinositide phosphatases.

Gregory S Taylor1, Jack E Dixon

  • 1Department of Pharmacology, University of California San Diego, La Jolla, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 3, 2004
PubMed
Summary

Researchers developed two new assays to study phosphoinositide phosphatases, crucial enzymes regulating cellular lipid signaling. These methods help understand enzyme activity and specificity in vital cell processes.

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

Emerging mechanisms of regulation for endoplasmic/sarcoplasmic reticulum Ca2+ stores by secretory pathway kinase FAM20C.

Current opinion in chemical biology·2023
Same author

Hippo pathway regulation by phosphatidylinositol transfer protein and phosphoinositides.

Nature chemical biology·2022
Same author

The ABCs of the atypical Fam20 secretory pathway kinases.

The Journal of biological chemistry·2021
Same author

The stress-responsive kinase DYRK2 activates heat shock factor 1 promoting resistance to proteotoxic stress.

Cell death and differentiation·2020
Same author

POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan.

eLife·2020
Same author

Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function.

Proceedings of the National Academy of Sciences of the United States of America·2019

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Signaling

Background:

  • Phosphoinositides are key signaling molecules involved in diverse cellular functions like growth, metabolism, and programmed cell death.
  • Understanding phosphoinositide regulation is crucial, yet novel signaling molecules highlight gaps in current knowledge.
  • Phosphoinositide phosphatases dephosphorylate these lipids, counteracting kinases and controlling cellular phosphoinositide levels.

Purpose of the Study:

  • To develop and present novel, rapid, and simple assays for characterizing phosphoinositide phosphatases.
  • To provide a foundational methodology for analyzing the activity and specificity of these enzymes.
  • To facilitate a deeper understanding of the enzymes that regulate cellular phosphoinositide homeostasis.

Main Methods:

  • Description of two newly developed assays for phosphoinositide phosphatase characterization.
  • Assays designed for speed and simplicity in experimental application.
  • Focus on enabling the assessment of enzyme activity and substrate specificity.

Main Results:

  • Successful development of two distinct assays for studying phosphoinositide phosphatases.
  • Demonstration of the assays' utility in characterizing enzyme activity.
  • Validation of the assays' capacity to assess enzyme specificity.

Conclusions:

  • The developed assays offer a valuable tool for the scientific community.
  • These methods will aid in elucidating the roles of phosphoinositide phosphatases in cellular signaling.
  • Further research into phosphoinositide metabolism can be advanced using these assays.

Related Experiment Videos