Prolyl isomerase Pin1 in cancer

Lu, Zhimin; Hunter, Tony

doi:10.1038/cr.2014.109

Cited by 160 publications

(226 citation statements)

References 135 publications

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“…ER␣ and Pin1 are important regulatory molecules in cell division and growth control that have overlapping and distinct roles in cancer (57,58). The growth-promoting activity of ER␣ is mediated through the transcriptional regulation of gene expression.…”

Section: Discussionmentioning

confidence: 99%

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Rajbhandari

Ozers

Solodin

et al. 2015

Journal of Biological Chemistry

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Background: Estrogen receptor ␣ (ER␣) activity in breast cancer cells is increased by Pin1, an isomerase that alters protein conformation. Results: Pin1-mediated isomerization increases ER␣ DNA binding affinity. Conclusion: Pin1 allosterically regulates ER␣ DNA binding directly via isomerization of phosphorylated receptor. Significance: Pin1 regulation of ER␣ provides a framework for understanding regulation by intrinsically disordered domains on transcription factor function.

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Section: Discussionmentioning

confidence: 99%

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Rajbhandari

Ozers

Solodin

et al. 2015

Journal of Biological Chemistry

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“…Upon EGFR activation, activated extracellular signal-regulated kinase 1 and 2 (ERK1/2) binds to the region that is encoded by exon 10 of PKM2 through a docking groove in ERK1/2, resulting in phosphorylation of S37 of PKM2, but not PKM1. Phosphorylated PKM2 then recruits peptidyl-prolyl cis-trans isomerase NIMAinteracting 1 (PIN1), which specifically catalyzes the cis-trans isomerization of peptide bonds between phosphorylated serine or threonine residues and proline residues (Lu and Hunter, 2014). This isomerization of PKM2 exposes its nuclear localization sequence (NLS) and promotes its binding to importin a5, which facilitates its nuclear translocation (Yang et al, 2012c).…”

Section: Regulation Of the Subcellular Localization Of Pkm2mentioning

confidence: 99%

Pyruvate kinase M2 at a glance

Yang

2015

Journal of Cell Science

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155

179

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Reprogrammed metabolism is a key feature of cancer cells. The pyruvate kinase M2 (PKM2) isoform, which is commonly upregulated in many human cancers, has been recently shown to play a crucial role in metabolism reprogramming, gene transcription and cell cycle progression. In this Cell Science at a glance article and accompanying poster, we provide a brief overview of recent advances in understanding the mechanisms underlying the regulation of PKM2 expression, enzymatic activity, metabolic functions and subcellular location. We highlight the instrumental role of the non-metabolic functions of PKM2 in tumorigenesis and evaluate the potential to target PKM2 for cancer treatment.

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“…Given that ssup-72(0) displays normal distal polyadenylation of unc-44, it is likely that the polyadenylation machinery at the internal 3′ end (PAS2) and the distal 3′ end (PAS3) differs in regulatory components. PINN-1, a conserved peptidyl prolyl isomerase, plays important roles in diverse cellular processes by mediating conformational changes of many proteins (Lu and Hunter, 2014). Our data reveal an in vivo role for PINN-1 in alternative polyadenylation.…”

Section: Discussionmentioning

confidence: 72%

Tissue-specific regulation of alternative polyadenylation represses expression of a neuronal ankyrin isoform in C. elegans epidermal development

2017

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Differential mRNA polyadenylation plays an important role in shaping the neuronal transcriptome. In C. elegans, several ankyrin isoforms are produced from the unc-44 locus through alternative polyadenylation. Here, we identify a key role for an intronic polyadenylation site (PAS) in temporal-and tissue-specific regulation of UNC-44/ankyrin isoforms. Removing an intronic PAS results in ectopic expression of the neuronal ankyrin isoform in non-neural tissues. This mis-expression underlies epidermal developmental defects in mutants of the conserved tumor suppressor death-associated protein kinase dapk-1. We have previously reported that the use of this intronic PAS depends on the nuclear polyadenylation factor SYDN-1, which inhibits the RNA polymerase II CTD phosphatase SSUP-72. Consistent with this, loss of sydn-1 blocks ectopic expression of neuronal ankyrin and suppresses epidermal morphology defects of dapk-1. These effects of sydn-1 are mediated by ssup-72 autonomously in the epidermis. We also show that a peptidyl-prolyl isomerase PINN-1 antagonizes SYDN-1 in the spatiotemporal control of neuronal ankyrin isoform. Moreover, the nuclear localization of PINN-1 is altered in dapk-1 mutants. Our data reveal that tissue and stage-specific expression of ankyrin isoforms relies on differential activity of positive and negative regulators of alternative polyadenylation.

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Prolyl isomerase Pin1 in cancer

Cited by 160 publications

References 135 publications

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α

Pyruvate kinase M2 at a glance

Tissue-specific regulation of alternative polyadenylation represses expression of a neuronal ankyrin isoform in C. elegans epidermal development

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