The Peptidyl-Prolyl Isomerase Pin1 Regulates Granulocyte-Macrophage Colony-Stimulating Factor mRNA Stability in T Lymphocytes

Esnault, Stéphane; Shen, Zhiquan; Whitesel, Emily; Malter, James S.

doi:10.4049/jimmunol.177.10.6999

Cited by 62 publications

(90 citation statements)

References 57 publications

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“…In addition, the observation that non-ARE-containing cytokine mRNAs can be regulated by AUF1 and HuR suggests considerable wobble in their target specificity. Previously we showed that Pin1 interacts with AUF1 and HuR in Eos and T cells and regulates the interaction of these AREBPs with GM-CSF mRNA (19,20). Here, we extended those observations by demonstrating a similar interaction between Pin1, AUF1, and TGF-β1 mRNA (Figure 8).…”

Section: Discussionsupporting

confidence: 73%

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Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis

Shen¹,

et al. 2008

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Eosinophilic inflammation is a cornerstone of chronic asthma that often culminates in subepithelial fibrosis with variable airway obstruction. Pulmonary eosinophils (Eos) are a predominant source of TGF-β1, which drives fibroblast proliferation and extracellular matrix deposition. We investigated the regulation of TGF-β1 and show here that the peptidyl-prolyl isomerase (PPIase) Pin1 promoted the stability of TGF-β1 mRNA in human Eos. In addition, Pin1 regulated cytokine production by both in vitro and in vivo activated human Eos. We found that Pin1 interacted with both PKC-α and protein phosphatase 2A, which together control Pin1 isomerase activity. Pharmacologic blockade of Pin1 in a rat asthma model selectively reduced eosinophilic pulmonary inflammation, TGF-β1 and collagen expression, and airway remodeling. Furthermore, chronically challenged Pin1 -/-mice showed reduced peribronchiolar collagen deposition compared with wild-type controls. These data suggest that pharmacologic suppression of Pin1 may be a novel therapeutic option to prevent airway fibrosis in individuals with chronic asthma.

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Section: Discussionsupporting

confidence: 73%

“…Recently, we have identified Pin1, a peptidyl-prolyl isomerase (PPIase), as a key regulator of inflammatory cytokine expression by activated Eos and T cells (19,20). Pin1 bound to and modulated the affinity of AUF1 for GM-CSF mRNA in response to external stimuli, leading to changes in GM-CSF mRNA decay, accumulation, and translation.…”

Section: Introductionmentioning

confidence: 99%

Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis

Shen¹,

et al. 2008

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“…Pin1 has also been shown to regulate the activity of AUF1 (10). There are a number of parallels in Pin1 regulation of histone mRNA metabolism via SLBP and the regulation of the GM-CSF mRNA decay via AUF1 (10).…”

Section: Discussionmentioning

confidence: 99%

“…Ess1 functionally interacts with the transcription initiation factor TFIIB, Ssu72 phosphatase, and Pta1 components of the 3=-end processing machinery to influence gene looping (24). Besides its effects on transcription, Pin1 has been implicated in the control of mRNA stability of three AU-rich element (ARE)-containing mRNAs, namely, those for granulocye-macrophage colony-stimulating factor (GM-CSF), parathyroid hormone (Pth), and transforming growth factor ␤ (TGF-␤), in the cytoplasm (10,25). These effects are mediated via direct association of Pin1 with phosphorylated forms of the ARE-binding proteins AUF1 and KSRP.…”

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confidence: 99%

The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination

Krishnan

Lam

Fritz

et al. 2012

Molecular and Cellular Biology

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f Histone mRNAs are rapidly degraded at the end of S phase, and a 26-nucleotide stem-loop in the 3= untranslated region is a key determinant of histone mRNA stability. This sequence is the binding site for stem-loop binding protein (SLBP), which helps to recruit components of the RNA degradation machinery to the histone mRNA 3= end. SLBP is the only protein whose expression is cell cycle regulated during S phase and whose degradation is temporally correlated with histone mRNA degradation. Here we report that chemical inhibition of the prolyl isomerase Pin1 or downregulation of Pin1 by small interfering RNA (siRNA) increases the mRNA stability of all five core histone mRNAs and the stability of SLBP. Pin1 regulates SLBP polyubiquitination via the Ser20/Ser23 phosphodegron in the N terminus. siRNA knockdown of Pin1 results in accumulation of SLBP in the nucleus. We show that Pin1 can act along with protein phosphatase 2A (PP2A) in vitro to dephosphorylate a phosphothreonine in a conserved TPNK sequence in the SLBP RNA binding domain, thereby dissociating SLBP from the histone mRNA hairpin. Our data suggest that Pin1 and PP2A act to coordinate the degradation of SLBP by the ubiquitin proteasome system and the exosomemediated degradation of the histone mRNA by regulating complex dissociation.

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“…Pin1 overexpression occurs in several types of cancer tissues (12), protects against the development of neurodegenerative disease (13), and may improve the outcomes of hepatitis B virus infection via physical interaction with hepatitis B virus X protein (14). Pin1 regulates the mRNA stability of TGF-␤ and GM-CSF in eosinophils and T lymphocytes (15)(16)(17). However, the pathological role of Pin1 in RA has not been studied.…”

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confidence: 99%

Novel Role of Pin1 Induction in Type II Collagen-Mediated Rheumatoid Arthritis

Jeong

Pokharel

Lim

et al. 2009

The Journal of Immunology

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Rheumatoid arthritis (RA) is an autoimmune disease characterized by chronic inflammation in joints and subsequent destruction of cartilage and bone. Inflammatory mediators such as PGs and proinflammatory cytokines contribute to RA progress. Pin1, a peptidyl prolyl isomerase, plays important pathophysiological roles in several diseases, including cancer and neurodegeneration. We found that both Pin1 and cyclooxygenase-2 (COX-2) were highly expressed in ankle tissues of type II collagen-induced RA mice. HTB-94 cells overexpressing Pin1 and primary cultured human chondrocytes showed increased basal expression of proinflammatory proteins (COX-2, inducible NO synthase, TNF-α, and IL-1β). Site-directed mutagenesis revealed that Pin1-mediated transcriptional activation of COX-2 was coordinately regulated by NF-κB, CREB, and C/EBP. Gel shift, reporter gene, and Western blot analyses confirmed that NF-κB, CREB, and C/EBP were consistently activated in chondrocytes overexpressing Pin1. Treatment of RA mice with juglone, a chemical inhibitor of Pin1, significantly reduced RA progress and COX-2 expression in the ankle tissues. Moreover, juglone dose dependently decreased the basal COX-2 expression in primary cultured chondrocytes from RA patients. These results demonstrate that Pin1 induction during RA progress stimulates proinflammatory protein expression by activating NF-κB, CREB, and C/EBP, and suggest that Pin1 is a potential therapeutic target of RA.

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The Peptidyl-Prolyl Isomerase Pin1 Regulates Granulocyte-Macrophage Colony-Stimulating Factor mRNA Stability in T Lymphocytes

Cited by 62 publications

References 57 publications

Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis

Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis

The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination

Novel Role of Pin1 Induction in Type II Collagen-Mediated Rheumatoid Arthritis

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