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Title: Native cytosolic protein phosphatase-1 (PP-1S) containing modulator (inhibitor-2) is an active enzyme
Authors: Bollen, Mathieu ×
DePaoli-Roach, A A
Stalmans, Willy #
Issue Date: Jun-1994
Series Title: FEBS Letters vol:344 issue:2-3 pages:196-200
Abstract: In vitro, the modulator protein (inhibitor-2) slowly converts the catalytic subunit of protein phosphatase-1 (PP-1C) into an inactive 'MgATP-dependent form' that can be reactivated by the transient phosphorylation of modulator with GSK-3/FA. We report here that this modulator-induced inactivation of PP-1C can be blocked by addition (at pH 7.5) of either 0.3 mM NaF or 150 mM NaCl, or by raising the pH to 8.5. Making use of a combination of the latter conditions, we have partially purified a soluble modulator-associated form of PP-1 (PP-1S) from rabbit skeletal muscle as a spontaneously active enzyme that cannot be further activated by kinase GSK-3/FA. These observations argue against a role for the 'MgATP-dependent' form of PP-1S as an inactive reservoir of PP-1C. PP-1S was separated on aminohexyl Sepharose from another active, cytosolic species of PP-1, which appears to be a proteolytic product of the glycogen-bound PP-1G.
URI: 
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Department of Cellular and Molecular Medicine - miscellaneous
Laboratory of Biosignaling & Therapeutics
× corresponding author
# (joint) last author

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