The scaffolding A/Tpd3 subunit and high phosphatase activity are dispensable for Cdc55 function in the Saccharomyces cerevisiae spindle checkpoint and in cytokinesis.

The Journal of Biological Chemistry
Roni KorenT Kleinberger

Abstract

Protein serine/threonine phosphatase 2A (PP2A) is a multifunctional enzyme whose trimeric form consists of a scaffolding A subunit, a catalytic C subunit, and one of several regulatory B subunits (B, B', and B''). The adenovirus E4orf4 protein associates with PP2A by directly binding the B or B' subunits. An interaction with an active PP2A containing the B subunit, or its homologue in yeast, Cdc55, is required for E4orf4-induced apoptosis in mammalian cells and for induction of growth arrest in Saccharomyces cerevisiae. In this work, Cdc55 was randomly mutagenized by low-fidelity PCR amplification, and Cdc55 mutants that lost the ability to transduce the E4orf4 toxic signal in yeast were selected. The mutations obtained by this protocol inhibited the association of Cdc55 with E4orf4, or with the PP2A-AC subunits, or both. Functional analysis revealed that a mutant that does not bind Tpd3, the yeast A subunit, as well as wild type Cdc55 in a tpd3Delta background, can form a heterodimer with the catalytic subunit. This association requires C subunit carboxyl methylation. The residual phosphatase activity associated with Cdc55 in the absence of Tpd3 is sufficient to maintain a partially active spindle checkpoint and to prevent cyt...Continue Reading

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Citations

Feb 1, 2012·Cell Research·Dries CastermansJohan M Thevelein
Jun 9, 2006·Microbiology and Molecular Biology Reviews : MMBR·Yu Jiang
Jul 1, 2008·Biochimica Et Biophysica Acta·Pieter J A EichhornRené Bernards
Feb 23, 2008·Trends in Biochemical Sciences·Veerle JanssensJozef Goris
Mar 30, 2007·Archives of Biochemistry and Biophysics·Sunny J-S YooPhilip A Gruppuso
May 28, 2005·Yeast
Oct 18, 2005·The Journal of Biological Chemistry·Tsofnat MaozTamar Kleinberger
Dec 4, 2020·Biomolecules·Perrine Goguet-RubioAnna Castro
Jul 28, 2013·Journal of Cell Science·Valentina RossioSatoshi Yoshida

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