Related Experiment Video
Updated: Jun 17, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
Published on: September 6, 2024
Regulation of type-1 protein phosphatase in a model of metabolic arrest
Christopher J Ramnanan1, Kenneth B Storey
1Vanderbilt University School of Medicine, Department of Molecular Physiology, 710 Robinson Research Building, 2200 Pierce Avenue, Nashville, TN 37232, USA. chris.ramnanan@vanderbilt.edu
Abstract:
Type-1 phosphatase (PP-1) was assessed in foot muscle (FM) and hepatopancreas (HP) of estivating (EST) Otala lactea. Snail PP-1 displayed several conserved traits, including sensitivity to inhibitors, substrate affinity, and reduction in size to a 39 kDa catalytic subunit (PP-1c). During EST, PP-1 activity in FM and HP crude extracts was reduced, though kinetics and protein levels of purified PP-1c isoforms were not altered. PP-1c protein levels increased and decreased in nuclear and glycogen-associated fractions, respectively, during EST. Gel filtration determined that a 257 kDa low K(m) PP-1alpha complex decreased during estivation whereas a 76 kDa high K(m) complex increased in EST. Western blotting confirmed that the 76 kDa protein consisted of PP-1alpha and nuclear inhibitor of PP-1 (NIPP-1). A suppression of PP-1 activity factors in the overall metabolic rate depression in estivating snails and the mechanism is mediated through altered cellular localization and interaction with binding partners.
More Related Videos
Related Concept Videos
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
PI3K/mTOR/AKT Signaling Pathway
Regulation of Metabolism
Amplifying Signals via Enzymatic Cascade
The JAK-STAT Signaling Pathway
mTOR Signaling and Cancer Progression
The mTOR pathway or the...

