CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
Membrane‐type 1 matrix metalloproteinase (MT1‐ MMP) localizes at the front of migrating cells and degrades the extracellular matrix barrier during cancer invasion. However, it is poorly understood how the polarized distribution of MT1‐MMP at the migration front is regulated. Here, we demonstrate tha...
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| Veröffentlicht in: | The EMBO journal 2002-08, Vol.21 (15), p.3949-3959 |
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| creator | Mori, Hidetoshi Tomari, Taizo Koshikawa, Naohiko Kajita, Masahiro Itoh, Yoshifumi Sato, Hiroshi Tojo, Hideaki Yana, Ikuo Seiki, Motoharu |
| description | Membrane‐type 1 matrix metalloproteinase (MT1‐ MMP) localizes at the front of migrating cells and degrades the extracellular matrix barrier during cancer invasion. However, it is poorly understood how the polarized distribution of MT1‐MMP at the migration front is regulated. Here, we demonstrate that MT1‐MMP forms a complex with CD44H via the hemopexin‐like (PEX) domain. A mutant MT1‐MMP lacking the PEX domain failed to bind CD44H and did not localize at the lamellipodia. The cytoplasmic tail of CD44H, which comprises interfaces that associate with the actin cytoskeleton, was important for its localization at lamellipodia. Overexpression of a CD44H mutant lacking the cytoplasmic tail also prevented MT1‐MMP from localizing at the lamellipodia. Modulation of F‐actin with cytochalasin D revealed that both CD44H and MT1‐MMP co‐localize closely with the actin cytoskeleton, dependent on the cytoplasmic tail of CD44H. Thus, CD44H appears to act as a linker that connects MT1‐MMP to the actin cytoskeleton and to play a role in directing MT1‐MMP to the migration front. The PEX domain of MT1‐MMP was indispensable in promoting cell migration and CD44H shedding. |
| doi_str_mv | 10.1093/emboj/cdf411 |
| format | Article |
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However, it is poorly understood how the polarized distribution of MT1‐MMP at the migration front is regulated. Here, we demonstrate that MT1‐MMP forms a complex with CD44H via the hemopexin‐like (PEX) domain. A mutant MT1‐MMP lacking the PEX domain failed to bind CD44H and did not localize at the lamellipodia. The cytoplasmic tail of CD44H, which comprises interfaces that associate with the actin cytoskeleton, was important for its localization at lamellipodia. Overexpression of a CD44H mutant lacking the cytoplasmic tail also prevented MT1‐MMP from localizing at the lamellipodia. Modulation of F‐actin with cytochalasin D revealed that both CD44H and MT1‐MMP co‐localize closely with the actin cytoskeleton, dependent on the cytoplasmic tail of CD44H. Thus, CD44H appears to act as a linker that connects MT1‐MMP to the actin cytoskeleton and to play a role in directing MT1‐MMP to the migration front. The PEX domain of MT1‐MMP was indispensable in promoting cell migration and CD44H shedding.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/cdf411</identifier><identifier>PMID: 12145196</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>actin ; Actins - analysis ; Animals ; CD44 ; Cell Membrane - metabolism ; Cell Movement - physiology ; Cercopithecus aethiops ; CHO Cells - cytology ; Cricetinae ; Cricetulus ; Cytoskeleton - metabolism ; Cytoskeleton - ultrastructure ; EMBO05 ; Fibroblasts - cytology ; Hemopexin - chemistry ; Humans ; Hyaluronan Receptors - chemistry ; Hyaluronan Receptors - genetics ; Hyaluronan Receptors - physiology ; invasion ; lamellipodium ; Macromolecular Substances ; Matrix Metalloproteinases, Membrane-Associated ; Metalloendopeptidases - metabolism ; MT1-MMP ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Protein Transport ; Pseudopodia - metabolism ; Recombinant Fusion Proteins - physiology ; Sequence Deletion ; Structure-Activity Relationship ; Transfection ; Tumor Cells, Cultured - cytology</subject><ispartof>The EMBO journal, 2002-08, Vol.21 (15), p.3949-3959</ispartof><rights>European Molecular Biology Organization 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Aug 01, 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5501-cb1f0aec203a7897b15e05aba061bda318e971ab068f2d0c87b54662df5b533b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC126155/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC126155/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12145196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mori, Hidetoshi</creatorcontrib><creatorcontrib>Tomari, Taizo</creatorcontrib><creatorcontrib>Koshikawa, Naohiko</creatorcontrib><creatorcontrib>Kajita, Masahiro</creatorcontrib><creatorcontrib>Itoh, Yoshifumi</creatorcontrib><creatorcontrib>Sato, Hiroshi</creatorcontrib><creatorcontrib>Tojo, Hideaki</creatorcontrib><creatorcontrib>Yana, Ikuo</creatorcontrib><creatorcontrib>Seiki, Motoharu</creatorcontrib><title>CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Membrane‐type 1 matrix metalloproteinase (MT1‐ MMP) localizes at the front of migrating cells and degrades the extracellular matrix barrier during cancer invasion. However, it is poorly understood how the polarized distribution of MT1‐MMP at the migration front is regulated. Here, we demonstrate that MT1‐MMP forms a complex with CD44H via the hemopexin‐like (PEX) domain. A mutant MT1‐MMP lacking the PEX domain failed to bind CD44H and did not localize at the lamellipodia. The cytoplasmic tail of CD44H, which comprises interfaces that associate with the actin cytoskeleton, was important for its localization at lamellipodia. Overexpression of a CD44H mutant lacking the cytoplasmic tail also prevented MT1‐MMP from localizing at the lamellipodia. Modulation of F‐actin with cytochalasin D revealed that both CD44H and MT1‐MMP co‐localize closely with the actin cytoskeleton, dependent on the cytoplasmic tail of CD44H. Thus, CD44H appears to act as a linker that connects MT1‐MMP to the actin cytoskeleton and to play a role in directing MT1‐MMP to the migration front. The PEX domain of MT1‐MMP was indispensable in promoting cell migration and CD44H shedding.</description><subject>actin</subject><subject>Actins - analysis</subject><subject>Animals</subject><subject>CD44</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Movement - physiology</subject><subject>Cercopithecus aethiops</subject><subject>CHO Cells - cytology</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Cytoskeleton - metabolism</subject><subject>Cytoskeleton - ultrastructure</subject><subject>EMBO05</subject><subject>Fibroblasts - cytology</subject><subject>Hemopexin - chemistry</subject><subject>Humans</subject><subject>Hyaluronan Receptors - chemistry</subject><subject>Hyaluronan Receptors - genetics</subject><subject>Hyaluronan Receptors - physiology</subject><subject>invasion</subject><subject>lamellipodium</subject><subject>Macromolecular Substances</subject><subject>Matrix Metalloproteinases, Membrane-Associated</subject><subject>Metalloendopeptidases - metabolism</subject><subject>MT1-MMP</subject><subject>Protein Interaction Mapping</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Pseudopodia - metabolism</subject><subject>Recombinant Fusion Proteins - physiology</subject><subject>Sequence Deletion</subject><subject>Structure-Activity Relationship</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured - cytology</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc2P0zAUxC0EYkvhxhVkceBEWL_YjpPDHqAsBbTABdSjZSdO690kDrbLtv89XlKV5UOcLNm_Gc97g9BjIC-BVPTU9NpdntZNywDuoBmwgmQ5EfwumpG8gIxBWZ2gByFcEkJ4KeA-OoEcGIeqmKGweMMYbqw3dQy4T2ZeDSaL-9FgwL2K3u7SdVRd50bvorGDCgZHhzvVm66zo2uswnqPVQiutiraYY2vbdxgmww3pnej2dkh6-yVwY3rlR0eonut6oJ5dDjn6Ovb8y-Ld9nF5-X7xauLrOacQFZraIkydU6oEmUlNHBDuNKKFKAbRaE0lQClSVG2eUPqUmjOiiJvWq45pZrO0dnkO251b5raDNGrTo7e9srvpVNW_v4y2I1cu-8S0t44T_rnB71337YmRNnbUKeh04bcNkgBFaMszxP47A_w0m39kGaTUPGcM5rAOXoxQbV3IXjTHoMAkTdNyp9NyqnJhD-9Hf4XfKguAXwCrm1n9v81k-cfX38QvGIFvTHOJl1IkmFt_K2w_w7yZOIHFbfeHD_6y8-GaHbHZ-WvZCGo4HL1aSlX5bISJadyRX8AlHLXKg</recordid><startdate>20020801</startdate><enddate>20020801</enddate><creator>Mori, Hidetoshi</creator><creator>Tomari, Taizo</creator><creator>Koshikawa, Naohiko</creator><creator>Kajita, Masahiro</creator><creator>Itoh, Yoshifumi</creator><creator>Sato, Hiroshi</creator><creator>Tojo, Hideaki</creator><creator>Yana, Ikuo</creator><creator>Seiki, Motoharu</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020801</creationdate><title>CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain</title><author>Mori, Hidetoshi ; Tomari, Taizo ; Koshikawa, Naohiko ; Kajita, Masahiro ; Itoh, Yoshifumi ; Sato, Hiroshi ; Tojo, Hideaki ; Yana, Ikuo ; Seiki, Motoharu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5501-cb1f0aec203a7897b15e05aba061bda318e971ab068f2d0c87b54662df5b533b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>actin</topic><topic>Actins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mori, Hidetoshi</au><au>Tomari, Taizo</au><au>Koshikawa, Naohiko</au><au>Kajita, Masahiro</au><au>Itoh, Yoshifumi</au><au>Sato, Hiroshi</au><au>Tojo, Hideaki</au><au>Yana, Ikuo</au><au>Seiki, Motoharu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2002-08-01</date><risdate>2002</risdate><volume>21</volume><issue>15</issue><spage>3949</spage><epage>3959</epage><pages>3949-3959</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Membrane‐type 1 matrix metalloproteinase (MT1‐ MMP) localizes at the front of migrating cells and degrades the extracellular matrix barrier during cancer invasion. However, it is poorly understood how the polarized distribution of MT1‐MMP at the migration front is regulated. Here, we demonstrate that MT1‐MMP forms a complex with CD44H via the hemopexin‐like (PEX) domain. A mutant MT1‐MMP lacking the PEX domain failed to bind CD44H and did not localize at the lamellipodia. The cytoplasmic tail of CD44H, which comprises interfaces that associate with the actin cytoskeleton, was important for its localization at lamellipodia. Overexpression of a CD44H mutant lacking the cytoplasmic tail also prevented MT1‐MMP from localizing at the lamellipodia. Modulation of F‐actin with cytochalasin D revealed that both CD44H and MT1‐MMP co‐localize closely with the actin cytoskeleton, dependent on the cytoplasmic tail of CD44H. Thus, CD44H appears to act as a linker that connects MT1‐MMP to the actin cytoskeleton and to play a role in directing MT1‐MMP to the migration front. The PEX domain of MT1‐MMP was indispensable in promoting cell migration and CD44H shedding.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12145196</pmid><doi>10.1093/emboj/cdf411</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | actin Actins - analysis Animals CD44 Cell Membrane - metabolism Cell Movement - physiology Cercopithecus aethiops CHO Cells - cytology Cricetinae Cricetulus Cytoskeleton - metabolism Cytoskeleton - ultrastructure EMBO05 Fibroblasts - cytology Hemopexin - chemistry Humans Hyaluronan Receptors - chemistry Hyaluronan Receptors - genetics Hyaluronan Receptors - physiology invasion lamellipodium Macromolecular Substances Matrix Metalloproteinases, Membrane-Associated Metalloendopeptidases - metabolism MT1-MMP Protein Interaction Mapping Protein Structure, Tertiary Protein Transport Pseudopodia - metabolism Recombinant Fusion Proteins - physiology Sequence Deletion Structure-Activity Relationship Transfection Tumor Cells, Cultured - cytology |
| title | CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain |
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