Landscape of Pin1 in the cell cycle

Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, ma...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Experimental biology and medicine (Maywood, N.J.) N.J.), 2015-03, Vol.240 (3), p.403-408
Hauptverfasser: Lin, Cheng-Han, Li, Hao-Yi, Lee, Yu-Cheng, Calkins, Marcus J, Lee, Kuen-Haur, Yang, Chia-Ning, Lu, Pei-Jung
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 408
container_issue 3
container_start_page 403
container_title Experimental biology and medicine (Maywood, N.J.)
container_volume 240
creator Lin, Cheng-Han
Li, Hao-Yi
Lee, Yu-Cheng
Calkins, Marcus J
Lee, Kuen-Haur
Yang, Chia-Ning
Lu, Pei-Jung
description Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle progression. The cell cycle disorder caused by dysregulation of these substrates is believed to be a common phenomenon in cancer. A number of recent studies have revealed possible functions of several important Pin1-binding cell cycle regulators. Investigating the involvement of Pin1 in the cell cycle may assist in the development of future cancer therapeutics. In this review, we summarize current knowledge regarding the network of Pin1 substrates and Pin1 regulators in cell cycle progression. In G1/S progression, cyclin D1, RB, p53, p27, and cyclin E are all well-known cell cycle regulators that are modulated by Pin1. During G2/M transition, our lab has shown that Aurora A suppresses Pin1 activity through phosphorylation at Ser16 and cooperates with hBora to modulate G2/M transition. We conclude that Pin1 may be thought of as a molecular timer which modulates cell cycle progression networks.
doi_str_mv 10.1177/1535370215570829
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4935233</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sage_id>10.1177_1535370215570829</sage_id><sourcerecordid>1666727097</sourcerecordid><originalsourceid>FETCH-LOGICAL-c500t-965b3a2b70e7e74c164cbeb5d0ce262ed48c13dcad196d6f84fc56e8f61f06153</originalsourceid><addsrcrecordid>eNp1UE1Lw0AQXUSxtXr3JAEvXqL7kZ3NXgQpfkFBD3peNptJm5JmazYp9N-b0g9U8DTDvDdv3jxCLhm9ZUypOyaFFIpyJqWiKddHZLgZxQK0Pt73PT4gZyHMKWVScTglAy4BuJZySK4nts6Ds0uMfBG9lzWLyjpqZxg5rKrIrV2F5-SksFXAi10dkc-nx4_xSzx5e34dP0xiJyltYw0yE5ZniqJClTgGicswkzl1yIFjnqSOidzZnGnIoUiTwknAtABWUOi9jsj9VnfZZQvMHdZtYyuzbMqFbdbG29L8RupyZqZ-ZRItJBeiF7jZCTT-q8PQmkUZNn_YGn0XDAMAxRXVqqfSLdU1PoQGi8MZRs0mW_M3237l6qe9w8I-zJ4QbwnBTtHMfdfUfVz_C34DTNmACA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1666727097</pqid></control><display><type>article</type><title>Landscape of Pin1 in the cell cycle</title><source>Access via SAGE</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Lin, Cheng-Han ; Li, Hao-Yi ; Lee, Yu-Cheng ; Calkins, Marcus J ; Lee, Kuen-Haur ; Yang, Chia-Ning ; Lu, Pei-Jung</creator><creatorcontrib>Lin, Cheng-Han ; Li, Hao-Yi ; Lee, Yu-Cheng ; Calkins, Marcus J ; Lee, Kuen-Haur ; Yang, Chia-Ning ; Lu, Pei-Jung</creatorcontrib><description>Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle progression. The cell cycle disorder caused by dysregulation of these substrates is believed to be a common phenomenon in cancer. A number of recent studies have revealed possible functions of several important Pin1-binding cell cycle regulators. Investigating the involvement of Pin1 in the cell cycle may assist in the development of future cancer therapeutics. In this review, we summarize current knowledge regarding the network of Pin1 substrates and Pin1 regulators in cell cycle progression. In G1/S progression, cyclin D1, RB, p53, p27, and cyclin E are all well-known cell cycle regulators that are modulated by Pin1. During G2/M transition, our lab has shown that Aurora A suppresses Pin1 activity through phosphorylation at Ser16 and cooperates with hBora to modulate G2/M transition. We conclude that Pin1 may be thought of as a molecular timer which modulates cell cycle progression networks.</description><identifier>ISSN: 1535-3702</identifier><identifier>EISSN: 1535-3699</identifier><identifier>DOI: 10.1177/1535370215570829</identifier><identifier>PMID: 25662955</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Cell Cycle - physiology ; Humans ; Minireviews ; NIMA-Interacting Peptidylprolyl Isomerase ; Peptidylprolyl Isomerase - physiology ; Phosphoproteins - physiology ; Signal Transduction - physiology</subject><ispartof>Experimental biology and medicine (Maywood, N.J.), 2015-03, Vol.240 (3), p.403-408</ispartof><rights>2015 by the Society for Experimental Biology and Medicine</rights><rights>2015 by the Society for Experimental Biology and Medicine.</rights><rights>2015 by the Society for Experimental Biology and Medicine 2015 The Society for Experimental Biology and Medicine</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-965b3a2b70e7e74c164cbeb5d0ce262ed48c13dcad196d6f84fc56e8f61f06153</citedby><cites>FETCH-LOGICAL-c500t-965b3a2b70e7e74c164cbeb5d0ce262ed48c13dcad196d6f84fc56e8f61f06153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4935233/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4935233/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,21819,27924,27925,43621,43622,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25662955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lin, Cheng-Han</creatorcontrib><creatorcontrib>Li, Hao-Yi</creatorcontrib><creatorcontrib>Lee, Yu-Cheng</creatorcontrib><creatorcontrib>Calkins, Marcus J</creatorcontrib><creatorcontrib>Lee, Kuen-Haur</creatorcontrib><creatorcontrib>Yang, Chia-Ning</creatorcontrib><creatorcontrib>Lu, Pei-Jung</creatorcontrib><title>Landscape of Pin1 in the cell cycle</title><title>Experimental biology and medicine (Maywood, N.J.)</title><addtitle>Exp Biol Med (Maywood)</addtitle><description>Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle progression. The cell cycle disorder caused by dysregulation of these substrates is believed to be a common phenomenon in cancer. A number of recent studies have revealed possible functions of several important Pin1-binding cell cycle regulators. Investigating the involvement of Pin1 in the cell cycle may assist in the development of future cancer therapeutics. In this review, we summarize current knowledge regarding the network of Pin1 substrates and Pin1 regulators in cell cycle progression. In G1/S progression, cyclin D1, RB, p53, p27, and cyclin E are all well-known cell cycle regulators that are modulated by Pin1. During G2/M transition, our lab has shown that Aurora A suppresses Pin1 activity through phosphorylation at Ser16 and cooperates with hBora to modulate G2/M transition. We conclude that Pin1 may be thought of as a molecular timer which modulates cell cycle progression networks.</description><subject>Cell Cycle - physiology</subject><subject>Humans</subject><subject>Minireviews</subject><subject>NIMA-Interacting Peptidylprolyl Isomerase</subject><subject>Peptidylprolyl Isomerase - physiology</subject><subject>Phosphoproteins - physiology</subject><subject>Signal Transduction - physiology</subject><issn>1535-3702</issn><issn>1535-3699</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1UE1Lw0AQXUSxtXr3JAEvXqL7kZ3NXgQpfkFBD3peNptJm5JmazYp9N-b0g9U8DTDvDdv3jxCLhm9ZUypOyaFFIpyJqWiKddHZLgZxQK0Pt73PT4gZyHMKWVScTglAy4BuJZySK4nts6Ds0uMfBG9lzWLyjpqZxg5rKrIrV2F5-SksFXAi10dkc-nx4_xSzx5e34dP0xiJyltYw0yE5ZniqJClTgGicswkzl1yIFjnqSOidzZnGnIoUiTwknAtABWUOi9jsj9VnfZZQvMHdZtYyuzbMqFbdbG29L8RupyZqZ-ZRItJBeiF7jZCTT-q8PQmkUZNn_YGn0XDAMAxRXVqqfSLdU1PoQGi8MZRs0mW_M3237l6qe9w8I-zJ4QbwnBTtHMfdfUfVz_C34DTNmACA</recordid><startdate>20150301</startdate><enddate>20150301</enddate><creator>Lin, Cheng-Han</creator><creator>Li, Hao-Yi</creator><creator>Lee, Yu-Cheng</creator><creator>Calkins, Marcus J</creator><creator>Lee, Kuen-Haur</creator><creator>Yang, Chia-Ning</creator><creator>Lu, Pei-Jung</creator><general>SAGE Publications</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150301</creationdate><title>Landscape of Pin1 in the cell cycle</title><author>Lin, Cheng-Han ; Li, Hao-Yi ; Lee, Yu-Cheng ; Calkins, Marcus J ; Lee, Kuen-Haur ; Yang, Chia-Ning ; Lu, Pei-Jung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c500t-965b3a2b70e7e74c164cbeb5d0ce262ed48c13dcad196d6f84fc56e8f61f06153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Cell Cycle - physiology</topic><topic>Humans</topic><topic>Minireviews</topic><topic>NIMA-Interacting Peptidylprolyl Isomerase</topic><topic>Peptidylprolyl Isomerase - physiology</topic><topic>Phosphoproteins - physiology</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Cheng-Han</creatorcontrib><creatorcontrib>Li, Hao-Yi</creatorcontrib><creatorcontrib>Lee, Yu-Cheng</creatorcontrib><creatorcontrib>Calkins, Marcus J</creatorcontrib><creatorcontrib>Lee, Kuen-Haur</creatorcontrib><creatorcontrib>Yang, Chia-Ning</creatorcontrib><creatorcontrib>Lu, Pei-Jung</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lin, Cheng-Han</au><au>Li, Hao-Yi</au><au>Lee, Yu-Cheng</au><au>Calkins, Marcus J</au><au>Lee, Kuen-Haur</au><au>Yang, Chia-Ning</au><au>Lu, Pei-Jung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Landscape of Pin1 in the cell cycle</atitle><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle><addtitle>Exp Biol Med (Maywood)</addtitle><date>2015-03-01</date><risdate>2015</risdate><volume>240</volume><issue>3</issue><spage>403</spage><epage>408</epage><pages>403-408</pages><issn>1535-3702</issn><eissn>1535-3699</eissn><abstract>Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle progression. The cell cycle disorder caused by dysregulation of these substrates is believed to be a common phenomenon in cancer. A number of recent studies have revealed possible functions of several important Pin1-binding cell cycle regulators. Investigating the involvement of Pin1 in the cell cycle may assist in the development of future cancer therapeutics. In this review, we summarize current knowledge regarding the network of Pin1 substrates and Pin1 regulators in cell cycle progression. In G1/S progression, cyclin D1, RB, p53, p27, and cyclin E are all well-known cell cycle regulators that are modulated by Pin1. During G2/M transition, our lab has shown that Aurora A suppresses Pin1 activity through phosphorylation at Ser16 and cooperates with hBora to modulate G2/M transition. We conclude that Pin1 may be thought of as a molecular timer which modulates cell cycle progression networks.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>25662955</pmid><doi>10.1177/1535370215570829</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1535-3702
ispartof Experimental biology and medicine (Maywood, N.J.), 2015-03, Vol.240 (3), p.403-408
issn 1535-3702
1535-3699
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4935233
source Access via SAGE; MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central
subjects Cell Cycle - physiology
Humans
Minireviews
NIMA-Interacting Peptidylprolyl Isomerase
Peptidylprolyl Isomerase - physiology
Phosphoproteins - physiology
Signal Transduction - physiology
title Landscape of Pin1 in the cell cycle
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T00%3A40%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Landscape%20of%20Pin1%20in%20the%20cell%20cycle&rft.jtitle=Experimental%20biology%20and%20medicine%20(Maywood,%20N.J.)&rft.au=Lin,%20Cheng-Han&rft.date=2015-03-01&rft.volume=240&rft.issue=3&rft.spage=403&rft.epage=408&rft.pages=403-408&rft.issn=1535-3702&rft.eissn=1535-3699&rft_id=info:doi/10.1177/1535370215570829&rft_dat=%3Cproquest_pubme%3E1666727097%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1666727097&rft_id=info:pmid/25662955&rft_sage_id=10.1177_1535370215570829&rfr_iscdi=true