5T4 Interacts with TIP-2/GIPC, a PDZ Protein, with Implications for Metastasis
Overexpression of the 5T4 transmembrane glycoprotein can have marked effects on both the actin cytoskeleton and cell migration. Using a yeast two-hybrid approach, we describe a novel interaction between 5T4 and TIP-2/GIPC, a cytoplasmic interacting protein containing a PDZ domain. The cytoplasmic ta...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2002-01, Vol.290 (3), p.1030-1036 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Awan, Abida Lucic, Melinda R. Shaw, David M. Sheppard, Freda Westwater, Caroline Lyons, Steve A. Stern, Peter L. |
| description | Overexpression of the 5T4 transmembrane glycoprotein can have marked effects on both the actin cytoskeleton and cell migration. Using a yeast two-hybrid approach, we describe a novel interaction between 5T4 and TIP-2/GIPC, a cytoplasmic interacting protein containing a PDZ domain. The cytoplasmic tail of 5T4 contains a class I PDZ-binding motif (Ser-Asp-Val) and we demonstrate that this region, in particular the terminal valine, is required for 5T4 interaction with TIP-2/GIPC. HeLa cells expressing hemagglutinin-tagged TIP-2/GIPC (HA-TIP-2/GIPC) have an altered distribution of endogenous 5T4, which colocalizes with HA-TIP-2/GIPC, thus supporting an interaction. Furthermore, TIP-2/GIPC can be coimmunoprecipitated with 5T4 from HeLa cell lysates. Identification of the 5T4 and TIP-2/GIPC interaction provides the first link between 5T4 and the actin cytoskeleton. Since other proteins, like 5T4, associate with TIP-2/GIPC and are linked with cancer, we explore the possibility that TIP-2/GIPC may be a common factor involved in the cancer process. |
| doi_str_mv | 10.1006/bbrc.2001.6288 |
| format | Article |
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Using a yeast two-hybrid approach, we describe a novel interaction between 5T4 and TIP-2/GIPC, a cytoplasmic interacting protein containing a PDZ domain. The cytoplasmic tail of 5T4 contains a class I PDZ-binding motif (Ser-Asp-Val) and we demonstrate that this region, in particular the terminal valine, is required for 5T4 interaction with TIP-2/GIPC. HeLa cells expressing hemagglutinin-tagged TIP-2/GIPC (HA-TIP-2/GIPC) have an altered distribution of endogenous 5T4, which colocalizes with HA-TIP-2/GIPC, thus supporting an interaction. Furthermore, TIP-2/GIPC can be coimmunoprecipitated with 5T4 from HeLa cell lysates. Identification of the 5T4 and TIP-2/GIPC interaction provides the first link between 5T4 and the actin cytoskeleton. Since other proteins, like 5T4, associate with TIP-2/GIPC and are linked with cancer, we explore the possibility that TIP-2/GIPC may be a common factor involved in the cancer process.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2001.6288</identifier><identifier>PMID: 11798178</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>actin ; Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Amino Acid Sequence ; Antigens, Neoplasm - chemistry ; Antigens, Neoplasm - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; cytoskeleton ; HeLa Cells ; Humans ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - immunology ; Membrane Glycoproteins - metabolism ; metastasis ; Microscopy, Fluorescence ; Molecular Sequence Data ; Neoplasm Metastasis ; Neuropeptides - chemistry ; Neuropeptides - metabolism ; oncofetal antigen ; Precipitin Tests ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Two-Hybrid System Techniques ; yeast two hybrid ; Yeasts - genetics</subject><ispartof>Biochemical and biophysical research communications, 2002-01, Vol.290 (3), p.1030-1036</ispartof><rights>2002 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-bb8e425aa065a83fc8c26b4f63c5c7b2edea04a2710b9e4fa425ff4fa67e0f883</citedby><cites>FETCH-LOGICAL-c340t-bb8e425aa065a83fc8c26b4f63c5c7b2edea04a2710b9e4fa425ff4fa67e0f883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X01962886$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11798178$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Awan, Abida</creatorcontrib><creatorcontrib>Lucic, Melinda R.</creatorcontrib><creatorcontrib>Shaw, David M.</creatorcontrib><creatorcontrib>Sheppard, Freda</creatorcontrib><creatorcontrib>Westwater, Caroline</creatorcontrib><creatorcontrib>Lyons, Steve A.</creatorcontrib><creatorcontrib>Stern, Peter L.</creatorcontrib><title>5T4 Interacts with TIP-2/GIPC, a PDZ Protein, with Implications for Metastasis</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Overexpression of the 5T4 transmembrane glycoprotein can have marked effects on both the actin cytoskeleton and cell migration. Using a yeast two-hybrid approach, we describe a novel interaction between 5T4 and TIP-2/GIPC, a cytoplasmic interacting protein containing a PDZ domain. The cytoplasmic tail of 5T4 contains a class I PDZ-binding motif (Ser-Asp-Val) and we demonstrate that this region, in particular the terminal valine, is required for 5T4 interaction with TIP-2/GIPC. HeLa cells expressing hemagglutinin-tagged TIP-2/GIPC (HA-TIP-2/GIPC) have an altered distribution of endogenous 5T4, which colocalizes with HA-TIP-2/GIPC, thus supporting an interaction. Furthermore, TIP-2/GIPC can be coimmunoprecipitated with 5T4 from HeLa cell lysates. Identification of the 5T4 and TIP-2/GIPC interaction provides the first link between 5T4 and the actin cytoskeleton. Since other proteins, like 5T4, associate with TIP-2/GIPC and are linked with cancer, we explore the possibility that TIP-2/GIPC may be a common factor involved in the cancer process.</description><subject>actin</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Antigens, Neoplasm - chemistry</subject><subject>Antigens, Neoplasm - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>cytoskeleton</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - immunology</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>metastasis</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Metastasis</subject><subject>Neuropeptides - chemistry</subject><subject>Neuropeptides - metabolism</subject><subject>oncofetal antigen</subject><subject>Precipitin Tests</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Homology, Amino Acid</subject><subject>Two-Hybrid System Techniques</subject><subject>yeast two hybrid</subject><subject>Yeasts - genetics</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM9LwzAUx4Mobk6vHqUnT2uXpGmbHmXqLEzdYYJ4CWn6gpH-mEmm-N-bsYEn4cH38D7vC--D0CXBCcE4n9W1VQnFmCQ55fwIjQkucUwJZsdojAMR05K8jtCZcx-BIiwvT9GIkKLkpOBj9JStWVT1HqxU3kXfxr9H62oV09miWs2nkYxWt2_Ryg4eTD_d76tu0xolvRl6F-nBRo_gpQtj3Dk60bJ1cHHICXq5v1vPH-Ll86Ka3yxjlTLs47rmwGgmJc4zyVOtuKJ5zXSeqkwVNYUGJGaSFgTXJTAtA6x1yLwArDlPJ-h637uxw-cWnBedcQraVvYwbJ0oCMMlZySAyR5UdnDOghYbazppfwTBYmdQ7AyKnUGxMxgOrg7N27qD5g8_KAsA3wMQ_vsyYIVTBnoFjbGgvGgG81_3L81pfhI</recordid><startdate>20020125</startdate><enddate>20020125</enddate><creator>Awan, Abida</creator><creator>Lucic, Melinda R.</creator><creator>Shaw, David M.</creator><creator>Sheppard, Freda</creator><creator>Westwater, Caroline</creator><creator>Lyons, Steve A.</creator><creator>Stern, Peter L.</creator><general>Elsevier Inc</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></search><sort><creationdate>20020125</creationdate><title>5T4 Interacts with TIP-2/GIPC, a PDZ Protein, with Implications for Metastasis</title><author>Awan, Abida ; 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Using a yeast two-hybrid approach, we describe a novel interaction between 5T4 and TIP-2/GIPC, a cytoplasmic interacting protein containing a PDZ domain. The cytoplasmic tail of 5T4 contains a class I PDZ-binding motif (Ser-Asp-Val) and we demonstrate that this region, in particular the terminal valine, is required for 5T4 interaction with TIP-2/GIPC. HeLa cells expressing hemagglutinin-tagged TIP-2/GIPC (HA-TIP-2/GIPC) have an altered distribution of endogenous 5T4, which colocalizes with HA-TIP-2/GIPC, thus supporting an interaction. Furthermore, TIP-2/GIPC can be coimmunoprecipitated with 5T4 from HeLa cell lysates. Identification of the 5T4 and TIP-2/GIPC interaction provides the first link between 5T4 and the actin cytoskeleton. 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| subjects | actin Adaptor Proteins, Signal Transducing Amino Acid Motifs Amino Acid Sequence Antigens, Neoplasm - chemistry Antigens, Neoplasm - metabolism Carrier Proteins - chemistry Carrier Proteins - metabolism cytoskeleton HeLa Cells Humans Membrane Glycoproteins - chemistry Membrane Glycoproteins - immunology Membrane Glycoproteins - metabolism metastasis Microscopy, Fluorescence Molecular Sequence Data Neoplasm Metastasis Neuropeptides - chemistry Neuropeptides - metabolism oncofetal antigen Precipitin Tests Protein Structure, Tertiary Sequence Homology, Amino Acid Two-Hybrid System Techniques yeast two hybrid Yeasts - genetics |
| title | 5T4 Interacts with TIP-2/GIPC, a PDZ Protein, with Implications for Metastasis |
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