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Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-β pathway.

Abstract：

:Protein phosphatases play a key role in balancing the cellular responses to the transforming growth factor-β (TGFβ) signals. Several protein phosphatases have been attributed roles in the regulation of the TGFβ pathway. Among these, PPM1A is the only phosphatase reported to dephosphorylate SMAD2/3 in the nucleus. However we observed PPM1A exclusively in the cytoplasmic fractions independently of TGFβ treatment in all cells tested. These observations imply that a bona fide nuclear SMAD2/3 phosphatase remains elusive. In this study, we report a role for protein phosphatase 5 (PP5) in the TGFβ pathway. We identified PP5 as an interactor of SMAD2/3. Interestingly, in mouse embryonic fibroblast cells derived from PP5-null mice, TGFβ-induced transcriptional responses were significantly enhanced. Rather surprisingly, this enhancement is due to the increased levels of SMAD3 protein observed in PP5-null MEFs compared to the wild type. No differences in the levels of SMAD3 transcripts were observed between the wild-type and PP5-null MEFs. While PP5 is capable of dephosphorylating SMAD3-tail in overexpression assays, we demonstrate that its activity is essential in controlling SMAD3 protein levels in MEFs. We propose that PP5 regulates the TGFβ pathway in MEFs by regulating the expression of SMAD3 protein levels.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Bruce DL,Macartney T,Yong W,Shou W,Sapkota GP

doi

10.1016/j.cellsig.2012.07.003

subject

Has Abstract

pub_date

2012-11-01 00:00:00

pages

1999-2006

issue

11

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(12)00193-3

journal_volume

24

pub_type

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