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

Mutations in yeast protein phosphatase type 1 that affect targeting subunit binding.

X Wu1, K Tatchell

  • 1Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, Louisiana 71130, USA.

Biochemistry
|June 20, 2001
PubMed
Summary

Protein phosphatase type 1 (PP1) interacts with regulatory subunits via a hydrophobic groove. This groove is crucial for PP1 function, localization, and substrate specificity, impacting cellular 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

A Gip1p-Glc7p phosphatase complex regulates septin organization and spore wall formation.

The Journal of cell biology·2001
Same author

Characterization of Gac1p, a regulatory subunit of protein phosphatase type I involved in glycogen accumulation in Saccharomyces cerevisiae.

Molecular genetics and genomics : MGG·2001
Same author

Hyperactive glycogen synthase mutants of Saccharomyces cerevisiae suppress the glc7-1 protein phosphatase mutant.

Journal of bacteriology·2001
Same author

Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.

Cell·2000
Same author

Anaphase spindle position is monitored by the BUB2 checkpoint.

Nature cell biology·2000
Same author

Protein phosphatase type-1 regulatory subunits Reg1p and Reg2p act as signal transducers in the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae.

Molecular & general genetics : MGG·2000

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Protein phosphatase type 1 (PP1) is a key enzyme regulating numerous cellular processes.
  • PP1 activity is modulated by regulatory subunits, often binding through a V/IXF motif to a hydrophobic groove on PP1.

Purpose of the Study:

  • To investigate the role of the PP1 hydrophobic groove in subunit interaction, biological activity, and substrate specificity.
  • To test the hypothesis that regulatory subunits bind to PP1 via its hydrophobic groove.

Main Methods:

  • Construction and analysis of 11 yeast PP1 (Glc7) variants with mutations in the hydrophobic groove.
  • Assessment of in vivo biological activity and in vitro catalytic activity.
  • Evaluation of binding affinity to regulatory subunits (Gac1, Reg1, Sds22).

Related Experiment Videos

Main Results:

  • Five PP1 variants showed impaired in vivo function despite in vitro catalytic activity.
  • Mutants exhibited reduced binding to V/IXF-motif containing subunits (Gac1, Reg1) but retained binding to Sds22.
  • One variant failed to localize to normal PP1 cellular compartments, and mutations affected substrate specificity.

Conclusions:

  • The hydrophobic groove of PP1 is essential for interaction with specific regulatory subunits.
  • This groove plays a critical role in PP1's subcellular localization and substrate specificity.
  • Understanding the hydrophobic groove's function is key to comprehending PP1 regulation.