Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer
Objectives Cancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled‐associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension...
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| Veröffentlicht in: | Cell proliferation 2021-03, Vol.54 (3), p.e12994-n/a |
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| creator | Hao, Leiyu Liu, Yan Yu, Xinqian Zhu, Yuerong Zhu, Yichao |
| description | Objectives
Cancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled‐associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension and BrCa cell motility. However, how Daam1 is involved in actin filament assembly and promotes pseudopodia formation in BrCa cells remains unclear.
Materials and methods
One hundred human BrCa samples were collected at Women's Hospital of Nanjing Medical University. Immunohistochemistry (IHC) was used to examine Daam1 and Fascin expression. Wound healing and Boyden chamber assays were used to explore cell migration and pseudopodia extension of BrCa cells. Co‐IP/pull down and Western blotting were performed to study the physical interaction between Daam1 and Fascin. Immunofluorescence assays were performed to observe whether Daam1 and Fascin were colocalized and mediated actin filament assembly.
Results
Fascin was upregulated in BrCa tissues compared with that in paracarcinoma tissues. The downregulation of Fascin caused a decline in pseudopodia formation and cell motility. Moreover, we found that Daam1 interacted with Fascin via formin homology (FH) domains, especially the FH2 domain. Immunofluorescence assays showed that Daam1 and Fascin partially colocalized to actin filaments, and the knockdown of Daam1 or Fascin failed to colocalize to short and curved actin filaments.
Conclusions
Daam1 specifically binds to Fascin via FH domains and cooperatively facilitates pseudopodia formation and cell migration by promoting actin filament assembly in BrCa.
Daam1 notably collaborates with Fascin to promote the assembly of actin filament, pseudopodia extension and cell migration. |
| doi_str_mv | 10.1111/cpr.12994 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_crossref_primary_10_1111_cpr_12994</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2498892827</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4714-3ba5b409707cdeb23167b831660def8405fedbb1c5a566c5e9fa8f1cbad5f7f13</originalsourceid><addsrcrecordid>eNp9ks2KFDEQgIMo7rh68AUk4EUPvZvfTnIRltFRYUERPYckncxm6e60SffKPIDvbdYeFxU0h4RKffWRIgXAU4zOcF3nbspnmCjF7oENpi1vCJbsPtgg1aJGCEJOwKNSrhHCFIv2ITihlHGpsNqA77uUhzjCqzSkPu0PsEuDiWOBKcDXxgwY2jh2cE5wZ4qroKmRS31vbMpmjje-P8Ap1-rZw6n4pUtT6qKBoXprPh0rfN_DIe7zelU9NntTZujM6Hx-DB4E0xf_5Hiegi-7N5-375rLD2_fby8uG8cEZg21hluGlEDCdd4SilthZd1b1PkgGeLBd9Zixw1vW8e9CkYG7KzpeBAB01PwavVOix185_w4Z9PrKcfB5INOJuo_M2O80vt0o4VimFBUBS-Ogpy-Lr7Meojltjkz-rQUTZiQQkgieEWf_4VepyWPtT1NJOEUtVL9n2JKSlVZUamXK-VyKiX7cPdkjPTtCOg6AvrnCFT22e893pG__rwC5yvwLfb-8G-T3n78tCp_AAGDvbk</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2498892827</pqid></control><display><type>article</type><title>Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Wiley Online Library Open Access</source><source>PubMed Central</source><creator>Hao, Leiyu ; Liu, Yan ; Yu, Xinqian ; Zhu, Yuerong ; Zhu, Yichao</creator><creatorcontrib>Hao, Leiyu ; Liu, Yan ; Yu, Xinqian ; Zhu, Yuerong ; Zhu, Yichao</creatorcontrib><description>Objectives
Cancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled‐associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension and BrCa cell motility. However, how Daam1 is involved in actin filament assembly and promotes pseudopodia formation in BrCa cells remains unclear.
Materials and methods
One hundred human BrCa samples were collected at Women's Hospital of Nanjing Medical University. Immunohistochemistry (IHC) was used to examine Daam1 and Fascin expression. Wound healing and Boyden chamber assays were used to explore cell migration and pseudopodia extension of BrCa cells. Co‐IP/pull down and Western blotting were performed to study the physical interaction between Daam1 and Fascin. Immunofluorescence assays were performed to observe whether Daam1 and Fascin were colocalized and mediated actin filament assembly.
Results
Fascin was upregulated in BrCa tissues compared with that in paracarcinoma tissues. The downregulation of Fascin caused a decline in pseudopodia formation and cell motility. Moreover, we found that Daam1 interacted with Fascin via formin homology (FH) domains, especially the FH2 domain. Immunofluorescence assays showed that Daam1 and Fascin partially colocalized to actin filaments, and the knockdown of Daam1 or Fascin failed to colocalize to short and curved actin filaments.
Conclusions
Daam1 specifically binds to Fascin via FH domains and cooperatively facilitates pseudopodia formation and cell migration by promoting actin filament assembly in BrCa.
Daam1 notably collaborates with Fascin to promote the assembly of actin filament, pseudopodia extension and cell migration.</description><identifier>ISSN: 0960-7722</identifier><identifier>EISSN: 1365-2184</identifier><identifier>DOI: 10.1111/cpr.12994</identifier><identifier>PMID: 33458919</identifier><language>eng</language><publisher>England: John Wiley & Sons, Inc</publisher><subject>Actin ; Actin Cytoskeleton - metabolism ; Adaptor Proteins, Signal Transducing - metabolism ; Antibodies ; Antigens ; Assaying ; Assembly ; Boyden chamber ; Breast cancer ; Breast Neoplasms - metabolism ; Breast Neoplasms - pathology ; Cell adhesion & migration ; Cell migration ; Cell Movement - physiology ; Cytoskeleton ; Dishevelled protein ; Domains ; Filaments ; Formins - metabolism ; Formins - pharmacology ; Homology ; Humans ; Immunofluorescence ; Immunohistochemistry ; Lung cancer ; Morphogenesis ; Motility ; Organs ; Original ; Ovarian cancer ; Penicillin ; Polymerization ; Proteins ; Pseudopodia ; Pseudopodia - metabolism ; Pseudopodia - pathology ; Reagents ; rho GTP-Binding Proteins - metabolism ; Western blotting ; Wound healing</subject><ispartof>Cell proliferation, 2021-03, Vol.54 (3), p.e12994-n/a</ispartof><rights>2021 The Authors. Published by John Wiley & Sons Ltd.</rights><rights>2021 The Authors. Cell Proliferation Published by John Wiley & Sons Ltd.</rights><rights>2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4714-3ba5b409707cdeb23167b831660def8405fedbb1c5a566c5e9fa8f1cbad5f7f13</citedby><cites>FETCH-LOGICAL-c4714-3ba5b409707cdeb23167b831660def8405fedbb1c5a566c5e9fa8f1cbad5f7f13</cites><orcidid>0000-0003-3499-8510</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7941230/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7941230/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,1413,11544,27906,27907,45556,45557,46034,46458,53773,53775</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33458919$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hao, Leiyu</creatorcontrib><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Yu, Xinqian</creatorcontrib><creatorcontrib>Zhu, Yuerong</creatorcontrib><creatorcontrib>Zhu, Yichao</creatorcontrib><title>Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer</title><title>Cell proliferation</title><addtitle>Cell Prolif</addtitle><description>Objectives
Cancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled‐associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension and BrCa cell motility. However, how Daam1 is involved in actin filament assembly and promotes pseudopodia formation in BrCa cells remains unclear.
Materials and methods
One hundred human BrCa samples were collected at Women's Hospital of Nanjing Medical University. Immunohistochemistry (IHC) was used to examine Daam1 and Fascin expression. Wound healing and Boyden chamber assays were used to explore cell migration and pseudopodia extension of BrCa cells. Co‐IP/pull down and Western blotting were performed to study the physical interaction between Daam1 and Fascin. Immunofluorescence assays were performed to observe whether Daam1 and Fascin were colocalized and mediated actin filament assembly.
Results
Fascin was upregulated in BrCa tissues compared with that in paracarcinoma tissues. The downregulation of Fascin caused a decline in pseudopodia formation and cell motility. Moreover, we found that Daam1 interacted with Fascin via formin homology (FH) domains, especially the FH2 domain. Immunofluorescence assays showed that Daam1 and Fascin partially colocalized to actin filaments, and the knockdown of Daam1 or Fascin failed to colocalize to short and curved actin filaments.
Conclusions
Daam1 specifically binds to Fascin via FH domains and cooperatively facilitates pseudopodia formation and cell migration by promoting actin filament assembly in BrCa.
Daam1 notably collaborates with Fascin to promote the assembly of actin filament, pseudopodia extension and cell migration.</description><subject>Actin</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Assaying</subject><subject>Assembly</subject><subject>Boyden chamber</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - metabolism</subject><subject>Breast Neoplasms - pathology</subject><subject>Cell adhesion & migration</subject><subject>Cell migration</subject><subject>Cell Movement - physiology</subject><subject>Cytoskeleton</subject><subject>Dishevelled protein</subject><subject>Domains</subject><subject>Filaments</subject><subject>Formins - metabolism</subject><subject>Formins - pharmacology</subject><subject>Homology</subject><subject>Humans</subject><subject>Immunofluorescence</subject><subject>Immunohistochemistry</subject><subject>Lung cancer</subject><subject>Morphogenesis</subject><subject>Motility</subject><subject>Organs</subject><subject>Original</subject><subject>Ovarian cancer</subject><subject>Penicillin</subject><subject>Polymerization</subject><subject>Proteins</subject><subject>Pseudopodia</subject><subject>Pseudopodia - metabolism</subject><subject>Pseudopodia - pathology</subject><subject>Reagents</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>Western blotting</subject><subject>Wound healing</subject><issn>0960-7722</issn><issn>1365-2184</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9ks2KFDEQgIMo7rh68AUk4EUPvZvfTnIRltFRYUERPYckncxm6e60SffKPIDvbdYeFxU0h4RKffWRIgXAU4zOcF3nbspnmCjF7oENpi1vCJbsPtgg1aJGCEJOwKNSrhHCFIv2ITihlHGpsNqA77uUhzjCqzSkPu0PsEuDiWOBKcDXxgwY2jh2cE5wZ4qroKmRS31vbMpmjje-P8Ap1-rZw6n4pUtT6qKBoXprPh0rfN_DIe7zelU9NntTZujM6Hx-DB4E0xf_5Hiegi-7N5-375rLD2_fby8uG8cEZg21hluGlEDCdd4SilthZd1b1PkgGeLBd9Zixw1vW8e9CkYG7KzpeBAB01PwavVOix185_w4Z9PrKcfB5INOJuo_M2O80vt0o4VimFBUBS-Ogpy-Lr7Meojltjkz-rQUTZiQQkgieEWf_4VepyWPtT1NJOEUtVL9n2JKSlVZUamXK-VyKiX7cPdkjPTtCOg6AvrnCFT22e893pG__rwC5yvwLfb-8G-T3n78tCp_AAGDvbk</recordid><startdate>202103</startdate><enddate>202103</enddate><creator>Hao, Leiyu</creator><creator>Liu, Yan</creator><creator>Yu, Xinqian</creator><creator>Zhu, Yuerong</creator><creator>Zhu, Yichao</creator><general>John Wiley & Sons, Inc</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</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>7QO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3499-8510</orcidid></search><sort><creationdate>202103</creationdate><title>Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer</title><author>Hao, Leiyu ; Liu, Yan ; Yu, Xinqian ; Zhu, Yuerong ; Zhu, Yichao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4714-3ba5b409707cdeb23167b831660def8405fedbb1c5a566c5e9fa8f1cbad5f7f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Actin</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>Assaying</topic><topic>Assembly</topic><topic>Boyden chamber</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - metabolism</topic><topic>Breast Neoplasms - pathology</topic><topic>Cell adhesion & migration</topic><topic>Cell migration</topic><topic>Cell Movement - physiology</topic><topic>Cytoskeleton</topic><topic>Dishevelled protein</topic><topic>Domains</topic><topic>Filaments</topic><topic>Formins - metabolism</topic><topic>Formins - pharmacology</topic><topic>Homology</topic><topic>Humans</topic><topic>Immunofluorescence</topic><topic>Immunohistochemistry</topic><topic>Lung cancer</topic><topic>Morphogenesis</topic><topic>Motility</topic><topic>Organs</topic><topic>Original</topic><topic>Ovarian cancer</topic><topic>Penicillin</topic><topic>Polymerization</topic><topic>Proteins</topic><topic>Pseudopodia</topic><topic>Pseudopodia - metabolism</topic><topic>Pseudopodia - pathology</topic><topic>Reagents</topic><topic>rho GTP-Binding Proteins - metabolism</topic><topic>Western blotting</topic><topic>Wound healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hao, Leiyu</creatorcontrib><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Yu, Xinqian</creatorcontrib><creatorcontrib>Zhu, Yuerong</creatorcontrib><creatorcontrib>Zhu, Yichao</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Wiley Online Library Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell proliferation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hao, Leiyu</au><au>Liu, Yan</au><au>Yu, Xinqian</au><au>Zhu, Yuerong</au><au>Zhu, Yichao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer</atitle><jtitle>Cell proliferation</jtitle><addtitle>Cell Prolif</addtitle><date>2021-03</date><risdate>2021</risdate><volume>54</volume><issue>3</issue><spage>e12994</spage><epage>n/a</epage><pages>e12994-n/a</pages><issn>0960-7722</issn><eissn>1365-2184</eissn><abstract>Objectives
Cancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled‐associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension and BrCa cell motility. However, how Daam1 is involved in actin filament assembly and promotes pseudopodia formation in BrCa cells remains unclear.
Materials and methods
One hundred human BrCa samples were collected at Women's Hospital of Nanjing Medical University. Immunohistochemistry (IHC) was used to examine Daam1 and Fascin expression. Wound healing and Boyden chamber assays were used to explore cell migration and pseudopodia extension of BrCa cells. Co‐IP/pull down and Western blotting were performed to study the physical interaction between Daam1 and Fascin. Immunofluorescence assays were performed to observe whether Daam1 and Fascin were colocalized and mediated actin filament assembly.
Results
Fascin was upregulated in BrCa tissues compared with that in paracarcinoma tissues. The downregulation of Fascin caused a decline in pseudopodia formation and cell motility. Moreover, we found that Daam1 interacted with Fascin via formin homology (FH) domains, especially the FH2 domain. Immunofluorescence assays showed that Daam1 and Fascin partially colocalized to actin filaments, and the knockdown of Daam1 or Fascin failed to colocalize to short and curved actin filaments.
Conclusions
Daam1 specifically binds to Fascin via FH domains and cooperatively facilitates pseudopodia formation and cell migration by promoting actin filament assembly in BrCa.
Daam1 notably collaborates with Fascin to promote the assembly of actin filament, pseudopodia extension and cell migration.</abstract><cop>England</cop><pub>John Wiley & Sons, Inc</pub><pmid>33458919</pmid><doi>10.1111/cpr.12994</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-3499-8510</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Open Access; PubMed Central |
| subjects | Actin Actin Cytoskeleton - metabolism Adaptor Proteins, Signal Transducing - metabolism Antibodies Antigens Assaying Assembly Boyden chamber Breast cancer Breast Neoplasms - metabolism Breast Neoplasms - pathology Cell adhesion & migration Cell migration Cell Movement - physiology Cytoskeleton Dishevelled protein Domains Filaments Formins - metabolism Formins - pharmacology Homology Humans Immunofluorescence Immunohistochemistry Lung cancer Morphogenesis Motility Organs Original Ovarian cancer Penicillin Polymerization Proteins Pseudopodia Pseudopodia - metabolism Pseudopodia - pathology Reagents rho GTP-Binding Proteins - metabolism Western blotting Wound healing |
| title | Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer |
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