Inhibitor-1 and -2 of PP2A have preference between PP2A complexes

Hirotsugu Hino; Kaori Takaki; Satoru Mochida

doi:10.1016/j.bbrc.2015.09.168

Inhibitor-1 and -2 of PP2A have preference between PP2A complexes

Hirotsugu Hino, Kaori Takaki, Satoru Mochida

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Protein phosphatase 2A (PP2A) forms tens of kinds of complexes with different substrate specificity and functions by using various regulatory B subunits. But how these complexes' activities are regulated separately is not well understood. Here we showed unequal enzyme inhibition of each form by two proteinous PP2A inhibitors, I1^PP2A and I2^PP2A. Immunoprecipitation assay using Xenopus egg extract showed that I1^PP2A bound B″/PR48, and I2^PP2A bound B56γ and B″/PR48 among four B subunits analyzed. Thus I1^PP2A and I2^PP2A seem to have B-subunit specificity. These results support the hypothesis that PP2A complexes containing common catalytic subunit are individually regulated for their separate functions in vivo.

Original language	English
Pages (from-to)	297-302
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	467
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2015.09.168
Publication status	Published - 13 Nov 2015
Externally published	Yes

Keywords

B-subunit specificity
I1
I2
Inhibitor protein
PP2A

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10.1016/j.bbrc.2015.09.168

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title = "Inhibitor-1 and -2 of PP2A have preference between PP2A complexes",

abstract = "Protein phosphatase 2A (PP2A) forms tens of kinds of complexes with different substrate specificity and functions by using various regulatory B subunits. But how these complexes' activities are regulated separately is not well understood. Here we showed unequal enzyme inhibition of each form by two proteinous PP2A inhibitors, I1PP2A and I2PP2A. Immunoprecipitation assay using Xenopus egg extract showed that I1PP2A bound B″/PR48, and I2PP2A bound B56γ and B″/PR48 among four B subunits analyzed. Thus I1PP2A and I2PP2A seem to have B-subunit specificity. These results support the hypothesis that PP2A complexes containing common catalytic subunit are individually regulated for their separate functions in vivo.",

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author = "Hirotsugu Hino and Kaori Takaki and Satoru Mochida",

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TY - JOUR

T1 - Inhibitor-1 and -2 of PP2A have preference between PP2A complexes

AU - Hino, Hirotsugu

AU - Takaki, Kaori

AU - Mochida, Satoru

PY - 2015/11/13

Y1 - 2015/11/13

N2 - Protein phosphatase 2A (PP2A) forms tens of kinds of complexes with different substrate specificity and functions by using various regulatory B subunits. But how these complexes' activities are regulated separately is not well understood. Here we showed unequal enzyme inhibition of each form by two proteinous PP2A inhibitors, I1PP2A and I2PP2A. Immunoprecipitation assay using Xenopus egg extract showed that I1PP2A bound B″/PR48, and I2PP2A bound B56γ and B″/PR48 among four B subunits analyzed. Thus I1PP2A and I2PP2A seem to have B-subunit specificity. These results support the hypothesis that PP2A complexes containing common catalytic subunit are individually regulated for their separate functions in vivo.

AB - Protein phosphatase 2A (PP2A) forms tens of kinds of complexes with different substrate specificity and functions by using various regulatory B subunits. But how these complexes' activities are regulated separately is not well understood. Here we showed unequal enzyme inhibition of each form by two proteinous PP2A inhibitors, I1PP2A and I2PP2A. Immunoprecipitation assay using Xenopus egg extract showed that I1PP2A bound B″/PR48, and I2PP2A bound B56γ and B″/PR48 among four B subunits analyzed. Thus I1PP2A and I2PP2A seem to have B-subunit specificity. These results support the hypothesis that PP2A complexes containing common catalytic subunit are individually regulated for their separate functions in vivo.

KW - B-subunit specificity

KW - I1

KW - I2

KW - Inhibitor protein

KW - PP2A

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DO - 10.1016/j.bbrc.2015.09.168

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SN - 0006-291X

VL - 467

SP - 297

EP - 302

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Inhibitor-1 and -2 of PP2A have preference between PP2A complexes

Abstract

Keywords

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