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2 results on '"C Wee Ong"'

1. Prolyl isomerase Pin1 downregulates tumor suppressor RUNX3 in breast cancer

Author

Kosei Ito, C Wee Ong, J-S Lim, Manuel Salto-Tellez, L-F Chen, Y-H Nicole Tsang, X-W Wu, and Yoshiaki Ito

Subjects
Cancer Research, RUNX3, tumor suppressor, Amino Acid Motifs, Down-Regulation, Breast Neoplasms, Biology, Molecular oncology, Article, breast cancer, Pin1, Breast cancer, Cell Line, Tumor, Genetics, medicine, Prolyl isomerase, Humans, Phosphorylation, NIMA-Interacting Peptidylprolyl Isomerase, skin and connective tissue diseases, Molecular Biology, degradation, Peptidylprolyl isomerase, Protein Stability, Tumor Suppressor Proteins, Ubiquitination, Cancer, Peptidylprolyl Isomerase, Cell cycle, medicine.disease, digestive system diseases, Core Binding Factor Alpha 3 Subunit, Cancer research, PIN1, Female
Abstract

Emerging evidence demonstrates that RUNX3 is a tumor suppressor in breast cancer. Inactivation of RUNX3 in mice results in spontaneous mammary gland tumors, and decreased or silenced expression of RUNX3 is frequently found in breast cancer cell lines and human breast cancer samples. However, the underlying mechanism for initiating RUNX3 inactivation in breast cancer remains elusive. Here, we identify prolyl-isomerase Pin1, which is often over-expressed in breast cancer, as a key regulator of RUNX3 inactivation. In human breast cancer cell lines and breast cancer samples, expression of Pin1 inversely correlates with the expression of RUNX3. In addition, Pin1 recognizes four phosphorylated Ser/Thr-Pro motifs in RUNX3 via its WW domain. Binding of Pin1 to RUNX3 suppresses the transcriptional activity of RUNX3. Furthermore, Pin1 reduces the cellular levels of RUNX3 in an isomerase activity-dependent manner by inducing the ubiquitination and proteasomal degradation of RUNX3. Knocking down Pin1 enhances the cellular levels and transcriptional activity of RUNX3 by inhibiting the ubiquitination and degradation of RUNX3. Our results identify Pin1 as a new regulator of RUNX3 inactivation in breast cancer.

Published
2012
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2. Prolyl isomerase Pin1 downregulates tumor suppressor RUNX3 in breast cancer.

Author

Nicole Tsang YH, Wu XW, Lim JS, Wee Ong C, Salto-Tellez M, Ito K, Ito Y, and Chen LF

Subjects
Amino Acid Motifs, Breast Neoplasms pathology, Cell Line, Tumor, Core Binding Factor Alpha 3 Subunit analysis, Core Binding Factor Alpha 3 Subunit chemistry, Core Binding Factor Alpha 3 Subunit genetics, Down-Regulation, Female, Humans, NIMA-Interacting Peptidylprolyl Isomerase, Peptidylprolyl Isomerase analysis, Phosphorylation, Protein Stability, Tumor Suppressor Proteins, Ubiquitination, Breast Neoplasms metabolism, Core Binding Factor Alpha 3 Subunit physiology, Peptidylprolyl Isomerase physiology
Abstract

Emerging evidence demonstrates that RUNX3 is a tumor suppressor in breast cancer. Inactivation of RUNX3 in mice results in spontaneous mammary gland tumors, and decreased or silenced expression of RUNX3 is frequently found in breast cancer cell lines and human breast cancer samples. However, the underlying mechanism for initiating RUNX3 inactivation in breast cancer remains elusive. Here, we identify prolyl isomerase Pin1, which is often overexpressed in breast cancer, as a key regulator of RUNX3 inactivation. In human breast cancer cell lines and breast cancer samples, expression of Pin1 inversely correlates with the expression of RUNX3. In addition, Pin1 recognizes four phosphorylated Ser/Thr-Pro motifs in RUNX3 via its WW domain. Binding of Pin1 to RUNX3 suppresses the transcriptional activity of RUNX3. Furthermore, Pin1 reduces the cellular levels of RUNX3 in an isomerase activity-dependent manner by inducing the ubiquitination and proteasomal degradation of RUNX3. Knocking down Pin1 enhances the cellular levels and transcriptional activity of RUNX3 by inhibiting the ubiquitination and degradation of RUNX3. Our results identify Pin1 as a new regulator of RUNX3 inactivation in breast cancer.

Published
2013
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