Angiomotin is a novel component of cadherin‐11/β‐catenin/p120 complex and is critical for cadherin‐11‐mediated cell migration. Issue 3 (2nd December 2014)
- Record Type:
- Journal Article
- Title:
- Angiomotin is a novel component of cadherin‐11/β‐catenin/p120 complex and is critical for cadherin‐11‐mediated cell migration. Issue 3 (2nd December 2014)
- Main Title:
- Angiomotin is a novel component of cadherin‐11/β‐catenin/p120 complex and is critical for cadherin‐11‐mediated cell migration
- Authors:
- Ortiz, Angelica
Lee, Yu‐Chen
Yu, Guoyu
Liu, Hsuan‐Chen
Lin, Song‐Chang
Bilen, Melmet Asim
Cho, Hyojin
Yu‐Lee, Li‐Yuan
Lin, Sue‐Hwa - Abstract:
- Abstract : Loss of E‐cadherin and up‐regulation of mesenchymal cadherins, a hallmark of the epithelial–mesenchymal transition, contributes to migration and dissemination of cancer cells. Expression of human cadherin‐11 (Cad11), also known as osteoblast cadherin, in prostate cancer increases the migration of prostate cancer cells. How Cad11 mediates cell migration is unknown. Using the human Cad11 cytoplasmic domain in pulldown assays, we identified human angiomotin (Amot), known to be involved in cell polarity, migration, and Hippo pathway, as a component of the Cad11 protein complex. Deletion analysis showed that the last C‐terminal 10 amino acids in Cad11 cytoplasmic domain are required for Amot binding. Further, Cad11 preferentially interacts with Amot‐p80 than Amot‐p130 isoform and binds directly to the middle domain of Amot‐p80. Cad11‐Amot interaction affects Cad11‐mediated cell migration, but not homophilic adhesion, as deletion of Amot binding motif of Cad11 (Cad11‐Δ Amot) did not abolish Cad11‐mediated cell–cell adhesion of mouse L cells, but significantly reduced Cad11‐mediated cell migration of human C4‐2B4 and PC3‐mm2 prostate cancer cells and human HEK293T cells. Together, our studies identified Amot‐p80 as a novel component of the Cad11 complex and demonstrated that Amot‐p80 is critical for Cad11‐mediated cell migration.—Ortiz, A., Lee, Y.‐C., Yu, G., Liu, H.‐C., Lin, S.‐C., Bilen, M. A., Cho, H., Yu‐Lee, L.‐Y., Lin, S.‐H. Angiomotin is a novel component ofAbstract : Loss of E‐cadherin and up‐regulation of mesenchymal cadherins, a hallmark of the epithelial–mesenchymal transition, contributes to migration and dissemination of cancer cells. Expression of human cadherin‐11 (Cad11), also known as osteoblast cadherin, in prostate cancer increases the migration of prostate cancer cells. How Cad11 mediates cell migration is unknown. Using the human Cad11 cytoplasmic domain in pulldown assays, we identified human angiomotin (Amot), known to be involved in cell polarity, migration, and Hippo pathway, as a component of the Cad11 protein complex. Deletion analysis showed that the last C‐terminal 10 amino acids in Cad11 cytoplasmic domain are required for Amot binding. Further, Cad11 preferentially interacts with Amot‐p80 than Amot‐p130 isoform and binds directly to the middle domain of Amot‐p80. Cad11‐Amot interaction affects Cad11‐mediated cell migration, but not homophilic adhesion, as deletion of Amot binding motif of Cad11 (Cad11‐Δ Amot) did not abolish Cad11‐mediated cell–cell adhesion of mouse L cells, but significantly reduced Cad11‐mediated cell migration of human C4‐2B4 and PC3‐mm2 prostate cancer cells and human HEK293T cells. Together, our studies identified Amot‐p80 as a novel component of the Cad11 complex and demonstrated that Amot‐p80 is critical for Cad11‐mediated cell migration.—Ortiz, A., Lee, Y.‐C., Yu, G., Liu, H.‐C., Lin, S.‐C., Bilen, M. A., Cho, H., Yu‐Lee, L.‐Y., Lin, S.‐H. Angiomotin is a novel component of cadherin‐11/β‐catenin/p120 complex and is critical for cadherin‐11‐mediated cell migration. FASEB J. 29, 1080–1091 (2015). www.fasebj.org … (more)
- Is Part Of:
- FASEB journal. Volume 29:Issue 3(2015)
- Journal:
- FASEB journal
- Issue:
- Volume 29:Issue 3(2015)
- Issue Display:
- Volume 29, Issue 3 (2015)
- Year:
- 2015
- Volume:
- 29
- Issue:
- 3
- Issue Sort Value:
- 2015-0029-0003-0000
- Page Start:
- 1080
- Page End:
- 1091
- Publication Date:
- 2014-12-02
- Subjects:
- adhesion -- E‐cadherin -- OB‐cadherin -- prostate
Biology -- Periodicals
Biology, Experimental -- Periodicals
570 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1096/fj.14-261594 ↗
- Languages:
- English
- ISSNs:
- 0892-6638
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13224.xml