Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex
Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cy...
Gespeichert in:
Veröffentlicht in: | Neurochemical research 2009-03, Vol.34 (3), p.438-444 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 444 |
---|---|
container_issue | 3 |
container_start_page | 438 |
container_title | Neurochemical research |
container_volume | 34 |
creator | CortEs, Joel Cerna Montalvo, Eliud Alfredo Garcia MuNiz, JesUs Mornet, Dominique Garrido, Efrain Centeno, Federico Cisneros, Bulmaro |
description | Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3- beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3- beta . Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3- beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3- beta is recruited to the beta 1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3- beta recruitment to the beta 1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f. |
doi_str_mv | 10.1007/s11064-008-9802-x |
format | Article |
fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_20420055</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>20420055</sourcerecordid><originalsourceid>FETCH-LOGICAL-p116t-a25ccd46346a73c885f14f14e3257b7a4a4576b31fbd17eb3e0f852f10178e693</originalsourceid><addsrcrecordid>eNotjEtLw0AUhQdRMFZ_gLtZuRu9d57JslStxargY10myY2N5GVmAv35BiocOPAdvsPYNcItAri7gAhWC4BUZClIcThhCRqnhM1AnbIE1LwqzOCcXYTwAzBbEhP2ej84rPhLX06NjxT4-uNZCZ5T9PydinGqY0td5LHncU9HjmLTRfoe644vyz2Fuu_4qm-Hhg6X7KzyTaCr_16wr8eHz9WT2L6tN6vlVgyINgovTVGU2iptvVNFmpoK9RxS0rjcee21cTZXWOUlOsoVQZUaWSGgS8lmasFujr_D2P9OFOKurUNBTeM76qewk6AlgDHqD84_UBQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20420055</pqid></control><display><type>article</type><title>Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex</title><source>SpringerLink Journals</source><creator>CortEs, Joel Cerna ; Montalvo, Eliud Alfredo Garcia ; MuNiz, JesUs ; Mornet, Dominique ; Garrido, Efrain ; Centeno, Federico ; Cisneros, Bulmaro</creator><creatorcontrib>CortEs, Joel Cerna ; Montalvo, Eliud Alfredo Garcia ; MuNiz, JesUs ; Mornet, Dominique ; Garrido, Efrain ; Centeno, Federico ; Cisneros, Bulmaro</creatorcontrib><description>Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3- beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3- beta . Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3- beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3- beta is recruited to the beta 1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3- beta recruitment to the beta 1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.</description><identifier>ISSN: 0364-3190</identifier><identifier>EISSN: 1573-6903</identifier><identifier>DOI: 10.1007/s11064-008-9802-x</identifier><language>eng</language><ispartof>Neurochemical research, 2009-03, Vol.34 (3), p.438-444</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>CortEs, Joel Cerna</creatorcontrib><creatorcontrib>Montalvo, Eliud Alfredo Garcia</creatorcontrib><creatorcontrib>MuNiz, JesUs</creatorcontrib><creatorcontrib>Mornet, Dominique</creatorcontrib><creatorcontrib>Garrido, Efrain</creatorcontrib><creatorcontrib>Centeno, Federico</creatorcontrib><creatorcontrib>Cisneros, Bulmaro</creatorcontrib><title>Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex</title><title>Neurochemical research</title><description>Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3- beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3- beta . Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3- beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3- beta is recruited to the beta 1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3- beta recruitment to the beta 1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.</description><issn>0364-3190</issn><issn>1573-6903</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNotjEtLw0AUhQdRMFZ_gLtZuRu9d57JslStxargY10myY2N5GVmAv35BiocOPAdvsPYNcItAri7gAhWC4BUZClIcThhCRqnhM1AnbIE1LwqzOCcXYTwAzBbEhP2ej84rPhLX06NjxT4-uNZCZ5T9PydinGqY0td5LHncU9HjmLTRfoe644vyz2Fuu_4qm-Hhg6X7KzyTaCr_16wr8eHz9WT2L6tN6vlVgyINgovTVGU2iptvVNFmpoK9RxS0rjcee21cTZXWOUlOsoVQZUaWSGgS8lmasFujr_D2P9OFOKurUNBTeM76qewk6AlgDHqD84_UBQ</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>CortEs, Joel Cerna</creator><creator>Montalvo, Eliud Alfredo Garcia</creator><creator>MuNiz, JesUs</creator><creator>Mornet, Dominique</creator><creator>Garrido, Efrain</creator><creator>Centeno, Federico</creator><creator>Cisneros, Bulmaro</creator><scope>7TK</scope></search><sort><creationdate>20090301</creationdate><title>Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex</title><author>CortEs, Joel Cerna ; Montalvo, Eliud Alfredo Garcia ; MuNiz, JesUs ; Mornet, Dominique ; Garrido, Efrain ; Centeno, Federico ; Cisneros, Bulmaro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p116t-a25ccd46346a73c885f14f14e3257b7a4a4576b31fbd17eb3e0f852f10178e693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CortEs, Joel Cerna</creatorcontrib><creatorcontrib>Montalvo, Eliud Alfredo Garcia</creatorcontrib><creatorcontrib>MuNiz, JesUs</creatorcontrib><creatorcontrib>Mornet, Dominique</creatorcontrib><creatorcontrib>Garrido, Efrain</creatorcontrib><creatorcontrib>Centeno, Federico</creatorcontrib><creatorcontrib>Cisneros, Bulmaro</creatorcontrib><collection>Neurosciences Abstracts</collection><jtitle>Neurochemical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CortEs, Joel Cerna</au><au>Montalvo, Eliud Alfredo Garcia</au><au>MuNiz, JesUs</au><au>Mornet, Dominique</au><au>Garrido, Efrain</au><au>Centeno, Federico</au><au>Cisneros, Bulmaro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex</atitle><jtitle>Neurochemical research</jtitle><date>2009-03-01</date><risdate>2009</risdate><volume>34</volume><issue>3</issue><spage>438</spage><epage>444</epage><pages>438-444</pages><issn>0364-3190</issn><eissn>1573-6903</eissn><abstract>Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3- beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3- beta . Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3- beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3- beta is recruited to the beta 1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3- beta recruitment to the beta 1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.</abstract><doi>10.1007/s11064-008-9802-x</doi><tpages>7</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0364-3190 |
ispartof | Neurochemical research, 2009-03, Vol.34 (3), p.438-444 |
issn | 0364-3190 1573-6903 |
language | eng |
recordid | cdi_proquest_miscellaneous_20420055 |
source | SpringerLink Journals |
title | Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T06%3A49%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Dp71f%20Modulates%20GSK3-%20beta%20Recruitment%20to%20the%20beta%201-Integrin%20Adhesion%20Complex&rft.jtitle=Neurochemical%20research&rft.au=CortEs,%20Joel%20Cerna&rft.date=2009-03-01&rft.volume=34&rft.issue=3&rft.spage=438&rft.epage=444&rft.pages=438-444&rft.issn=0364-3190&rft.eissn=1573-6903&rft_id=info:doi/10.1007/s11064-008-9802-x&rft_dat=%3Cproquest%3E20420055%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20420055&rft_id=info:pmid/&rfr_iscdi=true |