Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers

Prevalent overexpression of prolyl isomerase Pin1 in human cancers.

Phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr-Pro) is a major regulatory mechanism in cell proliferation and transformation. Interestingly, the pSer/Thr-Pro motifs in proteins exist in two distinct cis and trans conformations, whose conversion rate is normally reduced on phosphorylation, but is catalyzed specifically by the prolyl isomerase Pin1. Pin1 c...

The Peptidyl-Prolyl Isomerase Pin1 Regulates

Overexpression of the prolyl isomerase PIN1 promotes cell growth in osteosarcoma cells.

PIN1 was recently identified as a peptidyl-prolyl cis-trans isomerase (PPIase). It binds to and isomerizes specific pSer/Thr-Pro motifs and catalytically induces conformational changes after phosphorylation. PIN1 plays an important role in several cellular events, such as cell cycle progression, transcriptional regulation, RNA processing, cell pro...

Regulation of cardiac hypertrophic signaling by prolyl isomerase Pin1.

RATIONALE Cardiac hypertrophy results from the complex interplay of differentially regulated cascades based on the phosphorylation status of involved signaling molecules. Although numerous critical regulatory kinases and phosphatases have been identified in the myocardium, the intracellular mechanism for temporal regulation of signaling duration and intensity remains obscure. In the nonmyocyte ...

Pin1 prolyl isomerase regulates endothelial nitric oxide synthase.

OBJECTIVE The Pin1 prolyl isomerase acts in concert with proline-directed protein kinases to regulate function of protein substrates through isomerization of peptide bonds that link phosphoserine or phosphothreonine to proline. We sought to determine whether Pin1 interacts with endothelial nitric oxide synthase (eNOS) in endothelial cells in a manner that depends on proline-directed phosphoryla...