Dephosphorylation of CCAAT/enhancer-binding protein β by protein phosphatase 2A containing B56δ is required at the early time of adipogenesis

Park, Mi-Young; Choi, Yukyung; Lee, Hee Gu; Kim, Keun Il; Lim, Jong‐Seok; Oh, Ki-Sook; Yang, Young

doi:10.1016/j.bbalip.2014.08.008

Cited by 6 publications

(3 citation statements)

References 53 publications

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“…Furthermore, CCAAT/enhancer binding protein-β (C/EBP-β) was shown to be dephosphorylated by PP2A B56 , and this dephosphorylation is essential for adipogenesis of OP9 and 3T3-L1 cells (Park et al, 2014). Furthermore, CCAAT/enhancer binding protein-β (C/EBP-β) was shown to be dephosphorylated by PP2A B56 , and this dephosphorylation is essential for adipogenesis of OP9 and 3T3-L1 cells (Park et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…Various substrates of PP2A B56 have already been identified, including some cytosolic factors related to cell cycle progression or the Wnt signaling pathway. Furthermore, CCAAT/enhancer binding protein-β (C/EBP-β) was shown to be dephosphorylated by PP2A B56 , and this dephosphorylation is essential for adipogenesis of OP9 and 3T3-L1 cells (Park et al, 2014). Given that the mTORC1 pathway is also activated during adipogenesis, the dephosphorylation of C/EBP-β might be induced by mTORC1 activation.…”

Section: Discussionmentioning

confidence: 99%

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Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

et al. 2018

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Mammalian target of rapamycin complex 1 (mTORC1) kinase is a master regulator of the cellular response to nutrition-related signals such as insulin and amino acids. mTORC1 is activated on the lysosomal membrane and induces phosphorylation of a variety of downstream molecules. We previously showed that activated mTORC1 induces protein phosphatase 2A (PP2A)-mediated dephosphorylation of the transcription factor forkhead box K1 (FOXK1). The mechanism underlying the signal transduction from the cytoplasmic mTORC1 to the nuclear FOXK1 has remained unclear, however, we now show that a nuclear-cytoplasmic transport system is necessary for the mTORC1-FOXK1 signal transduction. This reaction is mediated by a shuttling protein B56, which is a regulatory subunit of PP2A and plays an essential role in the mTORC1-dependent dephosphorylation of FOXK1. These results suggest that PP2A phosphatase contributes to the signaling for mTORC1-dependent transcriptional regulation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

et al. 2018

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“…B56β and B56δ induce neural cell differentiation through the activation of nerve growth factor (NGF) signaling [ 10 ]. Loss-of-function studies showed that B56δ, but none of the other isoforms, dephosphorylates CCAAT/enhancer binding protein β (C/EBPβ) and thereby promotes adipogenesis [ 11 ]. B56β dephosphorylates and thereby inactivates Akt, a protein kinase central to multiple growth factor signaling pathways [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

A Nonsynonymous/Synonymous Substitution Analysis of the B56 Gene Family Aids in Understanding B56 Isoform Diversity

et al. 2015

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Gene duplication leads to the formation of gene families, wherein purifying or neutral selection maintains the original gene function, while diversifying selection confers new functions onto duplicated genes. The B56 gene family is highly conserved; it is encoded by one gene in protists and fungi, and five genes in vertebrates. B56 regulates protein phosphatase 2A (PP2A), an abundant heterotrimeric serine/threonine phosphatase that functions as a tumor suppressor and consists of a scaffolding “A” and catalytic “C” subunit heterodimer bound to a regulatory “B” subunit. Individual regulatory B56 subunits confer disparate functions onto PP2A in various cell-cell signaling pathways. B56 proteins share a conserved central core domain, but have divergent N- and C-termini which play a role in isoform specificity. We carried out a nonsynonymous/synonymous substitution analysis to better understand the divergence of vertebrate B56 genes. When five B56 paralogs from ten vertebrate species were analyzed, the gene family displayed purifying selection; stronger purifying selection was revealed when individual B56 isoforms were analyzed separately. The B56 core experienced stronger purifying selection than the N- and C-termini, which correlates with the presence of several contacts between the core and the AC heterodimer. Indeed, the majority of the contact points that we analyzed between B56 and the AC heterodimer experienced strong purifying selection. B56 subfamilies showed distinct patterns of selection in their N- and C-termini. The C-terminus of the B56-1 subfamily and the N-terminus of the B56-2 subfamily exhibited strong purifying selection, suggesting that these termini carry out subfamily-specific functions, while the opposite termini exhibited diversifying selection and likely carry out isoform-specific functions. We also found reduced synonymous substitutions at the N- and C-termini when grouping B56 genes by species but not by isoform, suggesting species-specific codon bias may have a role in regulating B56 gene expression.

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Phosphoprotein phosphatase 1CB (PPP1CB), a novel adipogenic activator, promotes 3T3-L1 adipogenesis

Cho

Min

Roh

et al. 2015

Biochemical and Biophysical Research Communications

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Dephosphorylation of CCAAT/enhancer-binding protein β by protein phosphatase 2A containing B56δ is required at the early time of adipogenesis

Cited by 6 publications

References 53 publications

Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

A Nonsynonymous/Synonymous Substitution Analysis of the B56 Gene Family Aids in Understanding B56 Isoform Diversity

Phosphoprotein phosphatase 1CB (PPP1CB), a novel adipogenic activator, promotes 3T3-L1 adipogenesis

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Dephosphorylation of CCAAT/enhancer-binding protein β by protein phosphatase 2A containing B56δ is required at the early time of adipogenesis

Cited by 6 publications

References 53 publications

Nuclear–cytoplasmic shuttling protein PP2AB56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

Nuclear–cytoplasmic shuttling protein PP2AB56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

A Nonsynonymous/Synonymous Substitution Analysis of the B56 Gene Family Aids in Understanding B56 Isoform Diversity

Phosphoprotein phosphatase 1CB (PPP1CB), a novel adipogenic activator, promotes 3T3-L1 adipogenesis

Contact Info

Product

Resources

About

Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1

Nuclear–cytoplasmic shuttling protein PP2A^B56 contributes to mTORC1‐dependent dephosphorylation of FOXK1