Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases
► We examine protein complexes containing insulin receptor substrates (IRSs). ► IRS-1 and IRS-2 form high-molecular-mass complexes with other proteins. ► Different complexes are formed depending on IRS-isoform, cell-type or stimulus. ► The complexes can modulate availability of IRSs to receptor tyro...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2011-01, Vol.404 (3), p.767-773 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 773 |
|---|---|
| container_issue | 3 |
| container_start_page | 767 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 404 |
| creator | Fukushima, Toshiaki Arai, Toshiya Ariga-Nedachi, Miyako Okajima, Hiroshi Ooi, Yuko Iijima, Yumi Sone, Meri Cho, Yoshitake Ando, Yasutoshi Kasahara, Kohei Ozoe, Atsufumi Yoshihara, Hidehito Chida, Kazuhiro Okada, Shigeru Kopchick, John J. Asano, Tomoichiro Hakuno, Fumihiko Takahashi, Shin-Ichiro |
| description | ► We examine protein complexes containing insulin receptor substrates (IRSs). ► IRS-1 and IRS-2 form high-molecular-mass complexes with other proteins. ► Different complexes are formed depending on IRS-isoform, cell-type or stimulus. ► The complexes can modulate availability of IRSs to receptor tyrosine kinases.
Insulin receptor substrates (IRSs) are phosphorylated by activated insulin/insulin-like growth factor (IGF)-I receptor tyrosine kinases. Phosphotyrosyl IRSs are recognized by signaling molecules possessing src homology region 2 (SH2) domains, which mediate various insulin/IGF bioactivities. However, we have shown that IRSs are also associated with other proteins by a phosphotyrosine-independent mechanism. Here, we demonstrated that IRSs form high-molecular-mass complexes (we named these complexes IRSomes) with various proteins and we elucidated their possible roles. Blue native-polyacrylamide gel electrophoresis of cell lysates revealed IRSome formation. Some proteins associated with IRSs in IRS-isoform-, cell-type-, or stimulus-specific manners. Results of the
in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-α. Also, tyrosine phosphorylation of IRS-2 by IGF-I receptor was increased when IRS-2 was contained in IRSomes prepared from FRTL-5 thyrocytes treated with dibutyryl cAMP. These results demonstrated that cytokine/hormone-induced formation of IRSomes modulates availability of IRSs to receptor tyrosine kinases. |
| doi_str_mv | 10.1016/j.bbrc.2010.12.045 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_847279533</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X10022837</els_id><sourcerecordid>847279533</sourcerecordid><originalsourceid>FETCH-LOGICAL-c423t-971ddd55e06a0b27ffb004140589ccdf9dede84dc9ad74b538e2dc0bca6087b23</originalsourceid><addsrcrecordid>eNp9kU1vEzEQhlcIRNPCH-AAvnHadOz9tMQFVVAiVeIAlbhZ_phNnHrXwfYW8nP4pzjaADdOI3ueed_RvEXxisKaAm2v92ulgl4zOH2wNdTNk2JFgUPJKNRPixUAtCXj9NtFcRnjHoDSuuXPiwtGadtXHFbFr80UZ2cnElDjIflA4qxiCjJhJIMPI9nZ7a4cvUM9OxnKUcZItB8PDn9mJO1kIqM3uZcwv9AGIh-ldVJZZ9ORJE_sYnF9rqWzD0i2wf9IOzJInU3LzT__dAw-2gnJg51kxPiieDZIF_HluV4V9x8_fL35VN59vt3cvL8rdc2qVPKOGmOaBqGVoFg3DAqgpjU0PdfaDNygwb42mkvT1aqpemRGg9Kyhb5TrLoq3i66h-C_zxiTGG3U6Jyc0M9R9HXHOt5UVSbZQuq8aQw4iEOwowxHQUGckhF7cUpGnJIRlImcTB56fZaf1Yjm78ifKDLwZgEG6YXcBhvF_Zes0MApxo7TTLxbCMxneLQYRNQWJ43G5uslYbz93wa_AddyroM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>847279533</pqid></control><display><type>article</type><title>Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Fukushima, Toshiaki ; Arai, Toshiya ; Ariga-Nedachi, Miyako ; Okajima, Hiroshi ; Ooi, Yuko ; Iijima, Yumi ; Sone, Meri ; Cho, Yoshitake ; Ando, Yasutoshi ; Kasahara, Kohei ; Ozoe, Atsufumi ; Yoshihara, Hidehito ; Chida, Kazuhiro ; Okada, Shigeru ; Kopchick, John J. ; Asano, Tomoichiro ; Hakuno, Fumihiko ; Takahashi, Shin-Ichiro</creator><creatorcontrib>Fukushima, Toshiaki ; Arai, Toshiya ; Ariga-Nedachi, Miyako ; Okajima, Hiroshi ; Ooi, Yuko ; Iijima, Yumi ; Sone, Meri ; Cho, Yoshitake ; Ando, Yasutoshi ; Kasahara, Kohei ; Ozoe, Atsufumi ; Yoshihara, Hidehito ; Chida, Kazuhiro ; Okada, Shigeru ; Kopchick, John J. ; Asano, Tomoichiro ; Hakuno, Fumihiko ; Takahashi, Shin-Ichiro</creatorcontrib><description>► We examine protein complexes containing insulin receptor substrates (IRSs). ► IRS-1 and IRS-2 form high-molecular-mass complexes with other proteins. ► Different complexes are formed depending on IRS-isoform, cell-type or stimulus. ► The complexes can modulate availability of IRSs to receptor tyrosine kinases.
Insulin receptor substrates (IRSs) are phosphorylated by activated insulin/insulin-like growth factor (IGF)-I receptor tyrosine kinases. Phosphotyrosyl IRSs are recognized by signaling molecules possessing src homology region 2 (SH2) domains, which mediate various insulin/IGF bioactivities. However, we have shown that IRSs are also associated with other proteins by a phosphotyrosine-independent mechanism. Here, we demonstrated that IRSs form high-molecular-mass complexes (we named these complexes IRSomes) with various proteins and we elucidated their possible roles. Blue native-polyacrylamide gel electrophoresis of cell lysates revealed IRSome formation. Some proteins associated with IRSs in IRS-isoform-, cell-type-, or stimulus-specific manners. Results of the
in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-α. Also, tyrosine phosphorylation of IRS-2 by IGF-I receptor was increased when IRS-2 was contained in IRSomes prepared from FRTL-5 thyrocytes treated with dibutyryl cAMP. These results demonstrated that cytokine/hormone-induced formation of IRSomes modulates availability of IRSs to receptor tyrosine kinases.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2010.12.045</identifier><identifier>PMID: 21168390</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3T3-L1 Cells ; adipocytes ; Adipocytes - metabolism ; Animals ; bioactive properties ; Bucladesine - metabolism ; cAMP ; gel electrophoresis ; HEK293 Cells ; Humans ; Insulin ; Insulin - metabolism ; Insulin receptor substrate (IRS) ; Insulin Receptor Substrate Proteins - metabolism ; insulin receptors ; Insulin-like growth factor (IGF) ; insulin-like growth factor I receptor ; Mice ; Multiprotein Complexes - metabolism ; Phosphorylation ; protein phosphorylation ; Receptor, IGF Type 1 - metabolism ; signal transducing adaptor proteins ; Thyroid Gland - cytology ; Thyroid Gland - metabolism ; Tumor necrosis factor (TNF)-α ; tumor necrosis factor-alpha ; Tumor Necrosis Factor-alpha - pharmacology ; tyrosine ; Tyrosine - metabolism ; Tyrosine phosphorylation</subject><ispartof>Biochemical and biophysical research communications, 2011-01, Vol.404 (3), p.767-773</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-971ddd55e06a0b27ffb004140589ccdf9dede84dc9ad74b538e2dc0bca6087b23</citedby><cites>FETCH-LOGICAL-c423t-971ddd55e06a0b27ffb004140589ccdf9dede84dc9ad74b538e2dc0bca6087b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2010.12.045$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21168390$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukushima, Toshiaki</creatorcontrib><creatorcontrib>Arai, Toshiya</creatorcontrib><creatorcontrib>Ariga-Nedachi, Miyako</creatorcontrib><creatorcontrib>Okajima, Hiroshi</creatorcontrib><creatorcontrib>Ooi, Yuko</creatorcontrib><creatorcontrib>Iijima, Yumi</creatorcontrib><creatorcontrib>Sone, Meri</creatorcontrib><creatorcontrib>Cho, Yoshitake</creatorcontrib><creatorcontrib>Ando, Yasutoshi</creatorcontrib><creatorcontrib>Kasahara, Kohei</creatorcontrib><creatorcontrib>Ozoe, Atsufumi</creatorcontrib><creatorcontrib>Yoshihara, Hidehito</creatorcontrib><creatorcontrib>Chida, Kazuhiro</creatorcontrib><creatorcontrib>Okada, Shigeru</creatorcontrib><creatorcontrib>Kopchick, John J.</creatorcontrib><creatorcontrib>Asano, Tomoichiro</creatorcontrib><creatorcontrib>Hakuno, Fumihiko</creatorcontrib><creatorcontrib>Takahashi, Shin-Ichiro</creatorcontrib><title>Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>► We examine protein complexes containing insulin receptor substrates (IRSs). ► IRS-1 and IRS-2 form high-molecular-mass complexes with other proteins. ► Different complexes are formed depending on IRS-isoform, cell-type or stimulus. ► The complexes can modulate availability of IRSs to receptor tyrosine kinases.
Insulin receptor substrates (IRSs) are phosphorylated by activated insulin/insulin-like growth factor (IGF)-I receptor tyrosine kinases. Phosphotyrosyl IRSs are recognized by signaling molecules possessing src homology region 2 (SH2) domains, which mediate various insulin/IGF bioactivities. However, we have shown that IRSs are also associated with other proteins by a phosphotyrosine-independent mechanism. Here, we demonstrated that IRSs form high-molecular-mass complexes (we named these complexes IRSomes) with various proteins and we elucidated their possible roles. Blue native-polyacrylamide gel electrophoresis of cell lysates revealed IRSome formation. Some proteins associated with IRSs in IRS-isoform-, cell-type-, or stimulus-specific manners. Results of the
in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-α. Also, tyrosine phosphorylation of IRS-2 by IGF-I receptor was increased when IRS-2 was contained in IRSomes prepared from FRTL-5 thyrocytes treated with dibutyryl cAMP. These results demonstrated that cytokine/hormone-induced formation of IRSomes modulates availability of IRSs to receptor tyrosine kinases.</description><subject>3T3-L1 Cells</subject><subject>adipocytes</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>bioactive properties</subject><subject>Bucladesine - metabolism</subject><subject>cAMP</subject><subject>gel electrophoresis</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Insulin</subject><subject>Insulin - metabolism</subject><subject>Insulin receptor substrate (IRS)</subject><subject>Insulin Receptor Substrate Proteins - metabolism</subject><subject>insulin receptors</subject><subject>Insulin-like growth factor (IGF)</subject><subject>insulin-like growth factor I receptor</subject><subject>Mice</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Phosphorylation</subject><subject>protein phosphorylation</subject><subject>Receptor, IGF Type 1 - metabolism</subject><subject>signal transducing adaptor proteins</subject><subject>Thyroid Gland - cytology</subject><subject>Thyroid Gland - metabolism</subject><subject>Tumor necrosis factor (TNF)-α</subject><subject>tumor necrosis factor-alpha</subject><subject>Tumor Necrosis Factor-alpha - pharmacology</subject><subject>tyrosine</subject><subject>Tyrosine - metabolism</subject><subject>Tyrosine phosphorylation</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1vEzEQhlcIRNPCH-AAvnHadOz9tMQFVVAiVeIAlbhZ_phNnHrXwfYW8nP4pzjaADdOI3ueed_RvEXxisKaAm2v92ulgl4zOH2wNdTNk2JFgUPJKNRPixUAtCXj9NtFcRnjHoDSuuXPiwtGadtXHFbFr80UZ2cnElDjIflA4qxiCjJhJIMPI9nZ7a4cvUM9OxnKUcZItB8PDn9mJO1kIqM3uZcwv9AGIh-ldVJZZ9ORJE_sYnF9rqWzD0i2wf9IOzJInU3LzT__dAw-2gnJg51kxPiieDZIF_HluV4V9x8_fL35VN59vt3cvL8rdc2qVPKOGmOaBqGVoFg3DAqgpjU0PdfaDNygwb42mkvT1aqpemRGg9Kyhb5TrLoq3i66h-C_zxiTGG3U6Jyc0M9R9HXHOt5UVSbZQuq8aQw4iEOwowxHQUGckhF7cUpGnJIRlImcTB56fZaf1Yjm78ifKDLwZgEG6YXcBhvF_Zes0MApxo7TTLxbCMxneLQYRNQWJ43G5uslYbz93wa_AddyroM</recordid><startdate>20110121</startdate><enddate>20110121</enddate><creator>Fukushima, Toshiaki</creator><creator>Arai, Toshiya</creator><creator>Ariga-Nedachi, Miyako</creator><creator>Okajima, Hiroshi</creator><creator>Ooi, Yuko</creator><creator>Iijima, Yumi</creator><creator>Sone, Meri</creator><creator>Cho, Yoshitake</creator><creator>Ando, Yasutoshi</creator><creator>Kasahara, Kohei</creator><creator>Ozoe, Atsufumi</creator><creator>Yoshihara, Hidehito</creator><creator>Chida, Kazuhiro</creator><creator>Okada, Shigeru</creator><creator>Kopchick, John J.</creator><creator>Asano, Tomoichiro</creator><creator>Hakuno, Fumihiko</creator><creator>Takahashi, Shin-Ichiro</creator><general>Elsevier Inc</general><scope>FBQ</scope><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></search><sort><creationdate>20110121</creationdate><title>Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases</title><author>Fukushima, Toshiaki ; Arai, Toshiya ; Ariga-Nedachi, Miyako ; Okajima, Hiroshi ; Ooi, Yuko ; Iijima, Yumi ; Sone, Meri ; Cho, Yoshitake ; Ando, Yasutoshi ; Kasahara, Kohei ; Ozoe, Atsufumi ; Yoshihara, Hidehito ; Chida, Kazuhiro ; Okada, Shigeru ; Kopchick, John J. ; Asano, Tomoichiro ; Hakuno, Fumihiko ; Takahashi, Shin-Ichiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-971ddd55e06a0b27ffb004140589ccdf9dede84dc9ad74b538e2dc0bca6087b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>3T3-L1 Cells</topic><topic>adipocytes</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>bioactive properties</topic><topic>Bucladesine - metabolism</topic><topic>cAMP</topic><topic>gel electrophoresis</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Insulin</topic><topic>Insulin - metabolism</topic><topic>Insulin receptor substrate (IRS)</topic><topic>Insulin Receptor Substrate Proteins - metabolism</topic><topic>insulin receptors</topic><topic>Insulin-like growth factor (IGF)</topic><topic>insulin-like growth factor I receptor</topic><topic>Mice</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Phosphorylation</topic><topic>protein phosphorylation</topic><topic>Receptor, IGF Type 1 - metabolism</topic><topic>signal transducing adaptor proteins</topic><topic>Thyroid Gland - cytology</topic><topic>Thyroid Gland - metabolism</topic><topic>Tumor necrosis factor (TNF)-α</topic><topic>tumor necrosis factor-alpha</topic><topic>Tumor Necrosis Factor-alpha - pharmacology</topic><topic>tyrosine</topic><topic>Tyrosine - metabolism</topic><topic>Tyrosine phosphorylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukushima, Toshiaki</creatorcontrib><creatorcontrib>Arai, Toshiya</creatorcontrib><creatorcontrib>Ariga-Nedachi, Miyako</creatorcontrib><creatorcontrib>Okajima, Hiroshi</creatorcontrib><creatorcontrib>Ooi, Yuko</creatorcontrib><creatorcontrib>Iijima, Yumi</creatorcontrib><creatorcontrib>Sone, Meri</creatorcontrib><creatorcontrib>Cho, Yoshitake</creatorcontrib><creatorcontrib>Ando, Yasutoshi</creatorcontrib><creatorcontrib>Kasahara, Kohei</creatorcontrib><creatorcontrib>Ozoe, Atsufumi</creatorcontrib><creatorcontrib>Yoshihara, Hidehito</creatorcontrib><creatorcontrib>Chida, Kazuhiro</creatorcontrib><creatorcontrib>Okada, Shigeru</creatorcontrib><creatorcontrib>Kopchick, John J.</creatorcontrib><creatorcontrib>Asano, Tomoichiro</creatorcontrib><creatorcontrib>Hakuno, Fumihiko</creatorcontrib><creatorcontrib>Takahashi, Shin-Ichiro</creatorcontrib><collection>AGRIS</collection><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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukushima, Toshiaki</au><au>Arai, Toshiya</au><au>Ariga-Nedachi, Miyako</au><au>Okajima, Hiroshi</au><au>Ooi, Yuko</au><au>Iijima, Yumi</au><au>Sone, Meri</au><au>Cho, Yoshitake</au><au>Ando, Yasutoshi</au><au>Kasahara, Kohei</au><au>Ozoe, Atsufumi</au><au>Yoshihara, Hidehito</au><au>Chida, Kazuhiro</au><au>Okada, Shigeru</au><au>Kopchick, John J.</au><au>Asano, Tomoichiro</au><au>Hakuno, Fumihiko</au><au>Takahashi, Shin-Ichiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2011-01-21</date><risdate>2011</risdate><volume>404</volume><issue>3</issue><spage>767</spage><epage>773</epage><pages>767-773</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>► We examine protein complexes containing insulin receptor substrates (IRSs). ► IRS-1 and IRS-2 form high-molecular-mass complexes with other proteins. ► Different complexes are formed depending on IRS-isoform, cell-type or stimulus. ► The complexes can modulate availability of IRSs to receptor tyrosine kinases.
Insulin receptor substrates (IRSs) are phosphorylated by activated insulin/insulin-like growth factor (IGF)-I receptor tyrosine kinases. Phosphotyrosyl IRSs are recognized by signaling molecules possessing src homology region 2 (SH2) domains, which mediate various insulin/IGF bioactivities. However, we have shown that IRSs are also associated with other proteins by a phosphotyrosine-independent mechanism. Here, we demonstrated that IRSs form high-molecular-mass complexes (we named these complexes IRSomes) with various proteins and we elucidated their possible roles. Blue native-polyacrylamide gel electrophoresis of cell lysates revealed IRSome formation. Some proteins associated with IRSs in IRS-isoform-, cell-type-, or stimulus-specific manners. Results of the
in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-α. Also, tyrosine phosphorylation of IRS-2 by IGF-I receptor was increased when IRS-2 was contained in IRSomes prepared from FRTL-5 thyrocytes treated with dibutyryl cAMP. These results demonstrated that cytokine/hormone-induced formation of IRSomes modulates availability of IRSs to receptor tyrosine kinases.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21168390</pmid><doi>10.1016/j.bbrc.2010.12.045</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2011-01, Vol.404 (3), p.767-773 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_847279533 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 3T3-L1 Cells adipocytes Adipocytes - metabolism Animals bioactive properties Bucladesine - metabolism cAMP gel electrophoresis HEK293 Cells Humans Insulin Insulin - metabolism Insulin receptor substrate (IRS) Insulin Receptor Substrate Proteins - metabolism insulin receptors Insulin-like growth factor (IGF) insulin-like growth factor I receptor Mice Multiprotein Complexes - metabolism Phosphorylation protein phosphorylation Receptor, IGF Type 1 - metabolism signal transducing adaptor proteins Thyroid Gland - cytology Thyroid Gland - metabolism Tumor necrosis factor (TNF)-α tumor necrosis factor-alpha Tumor Necrosis Factor-alpha - pharmacology tyrosine Tyrosine - metabolism Tyrosine phosphorylation |
| title | Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T05%3A11%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Insulin%20receptor%20substrates%20form%20high-molecular-mass%20complexes%20that%20modulate%20their%20availability%20to%20insulin/insulin-like%20growth%20factor-I%20receptor%20tyrosine%20kinases&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Fukushima,%20Toshiaki&rft.date=2011-01-21&rft.volume=404&rft.issue=3&rft.spage=767&rft.epage=773&rft.pages=767-773&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2010.12.045&rft_dat=%3Cproquest_cross%3E847279533%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=847279533&rft_id=info:pmid/21168390&rft_els_id=S0006291X10022837&rfr_iscdi=true |