The peptidyl–prolyl isomerase Pin1 regulates phospho-Ser77 retinoic acid receptor α stability

Vitamin A and retinoid signaling: genomic and nongenomic effects

“…Such PRMs bind proteins with SH3 or WW domains, the phosphorylation preventing or favoring the interaction (69)(70)(71). In line with this, the phosphorylated PRM of RAR ␣ has been shown to bind peptidyl-prolyl cis -trans isomerase never in mitosis A (NIMA)-interacting 1 (Pin1) ( 72,73 ), a WW domain-containing protein. In contrast, according to a recent study performed in our laboratory, the nonphosphorylated PRM of RAR ␥ interacts with vinexinß ( 74 ), an adaptor characterized by the presence of three SH3 domains.…”

“…Note, however, that the degradation of RAR ␣ has been correlated to the recruitment of Pin1 to the phosphorylated N-terminal PRM ( 72,73 ). Pin1 is well known to induce cis-trans isomerization of the proline residues that follow the phosphorylated serines in order to create new specifi c recognition sites for interacting factors ( 141 ), but the mechanism of the Pin1-mediated degradation of RAR ␣ remains to be defi ned.…”

Pin1 expression contributes to lung cancer prognosis and carcinogenesis

“…Pin1 expression may be an unfavorable prognostic factor in patients of NsCLC patients, and these results indicate that Pin1 may have a role in tumor development and metastasis and thus could serve as a novel target for treatment of NsCLC. [3][4][5][6][7] Pin1 is overexpressed in many different cancer types, including breast, prostate, lung, ovarian and cervical carcinomas, as well as melanoma and glioma. 4,8,9 Although the detailed molecular mechanism(s) remains to be elucidated, several studies have now implicated Pin1 in the genesis and malignancy of several cancer.…”

Cytosolic Aryl Sulfotransferase 4A1 Interacts with the Peptidyl Prolyl Cis-Trans Isomerase Pin1

“…B, isomerase-inactive Pin1 did not destabilize SULT4A1. FLAG-SULT4A1 was expressed with Pin1 (F) or the isomerase-inactive Pin1(C The degradation of some proteins such as c-Myc and Pim-1 is enhanced by Pin1 in a PP2A-dependent manner (Yeh et al, 2004;Brondani et al, 2005;Ma et al, 2007). PP2A may preferentially dephosphorylate phospho-serine/threonineproline motifs in the trans conformation (Fila et al, 2008).…”

“…Pin1-regulated degradation of many proteins involves polyubiquitination and subsequent degradation in the proteosomes (Yeh et al, 2004;Brondani et al, 2005;Ma et al, 2007). Therefore, we explored the degradation pathway for SULT4A1 in the presence of Pin1 by treating cells with the proteosome inhibitor MG132.…”