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Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and Significance.


ABSTRACT: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif and, subsequently, induces the conformational change of its substrates. Mounting evidence has demonstrated that Pin1 is widely overexpressed and/or overactivated in cancer, exerting a critical influence on tumor initiation and progression via regulation of the biological activity, protein degradation, or nucleus-cytoplasmic distribution of its substrates. Moreover, Pin1 participates in the cancer hallmarks through activating some oncogenes and growth enhancers, or inactivating some tumor suppressors and growth inhibitors, suggesting that Pin1 could be an attractive target for cancer therapy. In this review, we summarize the findings on the dysregulation, mechanisms, and biological functions of Pin1 in cancer cells, and also discuss the significance and potential applications of Pin1 dysregulation in human cancer.

SUBMITTER: Pu W 

PROVIDER: S-EPMC7136398 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and Significance.

Pu Wenchen W   Zheng Yuanyuan Y   Peng Yong Y  

Frontiers in cell and developmental biology 20200331


Peptidyl-prolyl <i>cis-trans</i> isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved and unique enzyme that specifically catalyzes the <i>cis-trans</i> isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif and, subsequently, induces the conformational change of its substrates. Mounting evidence has demonstrated that Pin1 is widely overexpressed and/or overactivated in cancer, exerting a critical influence on tumor initiation and progression via regulation of  ...[more]

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