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NTIS 바로가기Nature reviews. Cancer, v.7 no.5, 2007년, pp.381 - 388
Yeh, Elizabeth S. (Department of Cancer Biology, Abramson Family Cancer Research Institute, University of Pennsylvania, 4th floor BRB II) , Means, Anthony R. (6160, USA.)
PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and, based on gain- and loss-of-function studies, is presumed to operate as a molecular tim...
Curr. Top. Med. Chem. A Galat 3 1315 2003 10.2174/1568026033451862 Galat, A. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr. Top. Med. Chem. 3, 1315-1347 (2003).
Mol. Carcinog. KP Lu 45 397 2006 10.1002/mc.20216 Lu, K. P. et al. Targeting carcinogenesis: a role for the prolyl isomerase Pin1? Mol. Carcinog. 45, 397-402 (2006).
Nature L Pastorino 440 528 2006 10.1038/nature04543 Pastorino, L. et al. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production. Nature 440, 528-534 (2006).
Nature KP Lu 380 544 1996 10.1038/380544a0 Lu, K. P., Hanes, S. D. & Hunter, T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547 (1996). PIN1 is identified and described for the first time in mammals as a NIMA-interacting protein with a potential role as a negative regulator of mitosis.
Yeast SD Hanes 5 55 1989 10.1002/yea.320050108 Hanes, S. D., Shank, P. R. & Bostian, K. A. Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5, 55-72 (1989). ESS1P, the yeast PIN1 homologue, is described as an essential protein in yeast, a fact that did not hold true in mammalian systems.
EMBO J. DG Crenshaw 17 1315 1998 10.1093/emboj/17.5.1315 Crenshaw, D. G., Yang, J., Means, A. R. & Kornbluth, S. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17, 1315-1327 (1998).
Genes Dev. M Shen 12 706 1998 10.1101/gad.12.5.706 Shen, M., Stukenberg, P. T., Kirschner, M. W. & Lu, K. P. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12, 706-720 (1998).
Mol. Cell PT Stukenberg 7 1071 2001 10.1016/S1097-2765(01)00245-3 Stukenberg, P. T. & Kirschner, M. W. Pin1 acts catalytically to promote a conformational change in Cdc25. Mol. Cell 7, 1071-1083 (2001).
Science KE Winkler 287 1644 2000 10.1126/science.287.5458.1644 Winkler, K. E., Swenson, K. I., Kornbluth, S. & Means, A. R. Requirement of the prolyl isomerase Pin1 for the replication checkpoint. Science 287, 1644-1647 (2000).
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Biochem. Biophys. Res. Commun. F Fujimori 265 658 1999 10.1006/bbrc.1999.1736 Fujimori, F., Takahashi, K., Uchida, C. & Uchida, T. Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265, 658-663 (1999). The first of several papers to describe the germline deletion of PIN1. The only phenotype described in this publication was that PIN1-null were unable to efficiently re-enter the cell cycle from a quiescent state. Interestingly, no one has yet provided a direct mechanistic explanation for this phenomenon.
Gene R Maleszka 203 89 1997 10.1016/S0378-1119(97)00522-2 Maleszka, R., Lupas, A., Hanes, S. D. & Miklos, G. L. The dodo gene family encodes a novel protein involved in signal transduction and protein folding. Gene 203, 89-93 (1997).
Nature Cell Biol. T Hsu 3 538 2001 10.1038/35078508 Hsu, T., McRackan, D., Vincent, T. S. & Gert de Couet, H. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nature Cell Biol. 3, 538-543 (2001).
Proc. Natl Acad. Sci. USA YC Liou 99 1335 2002 10.1073/pnas.032404099 Liou, Y. C. et al. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Natl Acad. Sci. USA 99, 1335-1340 (2002). Describes notable phenotypes in Pin1 -deficient mice, and contains the first description of a non-mitotic target for PIN1.
Development FW Atchison 130 3579 2003 10.1242/dev.00584 Atchison, F. W., Capel, B. & Means, A. R. Pin1 regulates the timing of mammalian primordial germ cell proliferation. Development 130, 3579-3586 (2003). Elegantly describes how PIN1 can serve as a molecular 'timer' of G1/S progression, and shows that the lack of this function in the PIN1-null mouse leads to fewer divisions of the primordial germ cells and thus to infertility.
Biol. Reprod. FW Atchison 69 1989 2003 10.1095/biolreprod.103.020859 Atchison, F. W. & Means, A. R. Spermatogonial depletion in adult Pin1-deficient mice. Biol. Reprod. 69, 1989-1997 (2003).
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J. Biol. Chem. JD Joseph 279 32373 2004 10.1074/jbc.M405415200 Joseph, J. D., Daigle, S. N. & Means, A. R. PINA is essential for growth and positively influences NIMA function in Aspergillus nidulans. J. Biol. Chem. 279, 32373-32384 (2004).
Mol. Cell Biol. A Ryo 22 5281 2002 10.1128/MCB.22.15.5281-5295.2002 Ryo, A. et al. PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell Biol. 22, 5281-5295 (2002).
J. Biol. Chem. ES Yeh 281 241 2006 10.1074/jbc.M505770200 Yeh, E. S., Lew, B. O. & Means, A. R. The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability. J. Biol. Chem. 281, 241-251 (2006).
Nature Cell Biol. A Ryo 3 793 2001 10.1038/ncb0901-793 Ryo, A., Nakamura, M., Wulf, G., Liou, Y. C. & Lu, K. P. Pin1 regulates turnover and subcellular localization of b-catenin by inhibiting its interaction with APC. Nature Cell Biol. 3, 793-801 (2001).
EMBO J. GM Wulf 20 3459 2001 10.1093/emboj/20.13.3459 Wulf, G. M. et al. Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. EMBO J. 20, 3459-3472 (2001). The first paper to suggest that PIN1 might act as a tumour-promoting factor. The authors provide data that shows that PIN1 is upregulated in human tumour samples.
Nature Cell Biol. E Yeh 6 308 2004 10.1038/ncb1110 Yeh, E. et al. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nature Cell Biol. 6, 308-318 (2004). This paper provides a detailed molecular mechanism of how PIN1 regulates the stability of one of its important G1 targets, MYC, as well as the first data suggesting the possibility that PIN1 may act as a tumour suppressor.
Mol. Cell F Mantovani 14 625 2004 10.1016/j.molcel.2004.05.007 Mantovani, F. et al. Pin1 links the activities of c-Abl and p300 in regulating p73 function. Mol. Cell 14, 625-636 (2004).
Nature P Zacchi 419 853 2002 10.1038/nature01120 Zacchi, P. et al. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419, 853-857 (2002).
Nature H Zheng 419 849 2002 10.1038/nature01116 Zheng, H. et al. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 419, 849-853 (2002). An important set of publications that identify p53 as a target of PIN1 and demonstrate that p53 is regulated by PIN1 in response to cell stress. PIN1 is shown to be required for p53 stabilization, which is necessary for its activity as a transcription factor.
Mol. Cell MK Dougherty 17 215 2005 10.1016/j.molcel.2004.11.055 Dougherty, M. K. et al. Regulation of Raf-1 by direct feedback phosphorylation. Mol. Cell 17, 215-224 (2005).
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Cancer Res. G Ayala 63 6244 2003 Ayala, G. et al. The prolyl isomerase Pin1 is a novel prognostic marker in human prostate cancer. Cancer Res. 63, 6244-6251 (2003).
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Mol. Cell. Biol. SY Chen 26 929 2006 10.1128/MCB.26.3.929-939.2006 Chen, S. Y. et al. Activation of β-catenin signaling in prostate cancer by peptidyl-prolyl isomerase Pin1-mediated abrogation of the androgen receptor-β-catenin interaction. Mol. Cell. Biol. 26, 929-939 (2006).
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