LINKIN, a new transmembrane protein necessary for cell adhesion
In epithelial collective migration, leader and follower cells migrate while maintaining cell–cell adhesion and tissue polarity. We have identified a conserved protein and interactors required for maintaining cell adhesion during a simple collective migration in the developing C. elegans male gonad....
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Format: | Article |
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eLife Sciences Publications Ltd
2014-12-01
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Series: | eLife |
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Online Access: | https://elifesciences.org/articles/04449 |
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author | Mihoko Kato Tsui-Fen Chou Collin Z Yu John DeModena Paul W Sternberg |
author_facet | Mihoko Kato Tsui-Fen Chou Collin Z Yu John DeModena Paul W Sternberg |
author_sort | Mihoko Kato |
collection | DOAJ |
description | In epithelial collective migration, leader and follower cells migrate while maintaining cell–cell adhesion and tissue polarity. We have identified a conserved protein and interactors required for maintaining cell adhesion during a simple collective migration in the developing C. elegans male gonad. LINKIN is a previously uncharacterized, transmembrane protein conserved throughout Metazoa. We identified seven atypical FG–GAP domains in the extracellular domain, which potentially folds into a β-propeller structure resembling the α-integrin ligand-binding domain. C. elegans LNKN-1 localizes to the plasma membrane of all gonadal cells, with apical and lateral bias. We identified the LINKIN interactors RUVBL1, RUVBL2, and α-tubulin by using SILAC mass spectrometry on human HEK 293T cells and testing candidates for lnkn-1-like function in C. elegans male gonad. We propose that LINKIN promotes adhesion between neighboring cells through its extracellular domain and regulates microtubule dynamics through RUVBL proteins at its intracellular domain. |
first_indexed | 2024-04-14T07:45:44Z |
format | Article |
id | doaj.art-ffc3dfb87e8c41dead5b003126f43066 |
institution | Directory Open Access Journal |
issn | 2050-084X |
language | English |
last_indexed | 2024-04-14T07:45:44Z |
publishDate | 2014-12-01 |
publisher | eLife Sciences Publications Ltd |
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series | eLife |
spelling | doaj.art-ffc3dfb87e8c41dead5b003126f430662022-12-22T02:05:20ZengeLife Sciences Publications LtdeLife2050-084X2014-12-01310.7554/eLife.04449LINKIN, a new transmembrane protein necessary for cell adhesionMihoko Kato0Tsui-Fen Chou1Collin Z Yu2John DeModena3Paul W Sternberg4https://orcid.org/0000-0002-7699-0173Division of Biology and Biological Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Biology and Biological Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United States; Division of Medical Genetics, Department of Pediatrics, Harbor-UCLA Medical Center, Torrance, United States; Los Angeles Biomedical Research Institute, Torrance, United StatesDivision of Biology and Biological Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Biology and Biological Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Biology and Biological Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesIn epithelial collective migration, leader and follower cells migrate while maintaining cell–cell adhesion and tissue polarity. We have identified a conserved protein and interactors required for maintaining cell adhesion during a simple collective migration in the developing C. elegans male gonad. LINKIN is a previously uncharacterized, transmembrane protein conserved throughout Metazoa. We identified seven atypical FG–GAP domains in the extracellular domain, which potentially folds into a β-propeller structure resembling the α-integrin ligand-binding domain. C. elegans LNKN-1 localizes to the plasma membrane of all gonadal cells, with apical and lateral bias. We identified the LINKIN interactors RUVBL1, RUVBL2, and α-tubulin by using SILAC mass spectrometry on human HEK 293T cells and testing candidates for lnkn-1-like function in C. elegans male gonad. We propose that LINKIN promotes adhesion between neighboring cells through its extracellular domain and regulates microtubule dynamics through RUVBL proteins at its intracellular domain.https://elifesciences.org/articles/04449human cellcell migrationorganogenesiscell polarityprotein-protein interaction |
spellingShingle | Mihoko Kato Tsui-Fen Chou Collin Z Yu John DeModena Paul W Sternberg LINKIN, a new transmembrane protein necessary for cell adhesion eLife human cell cell migration organogenesis cell polarity protein-protein interaction |
title | LINKIN, a new transmembrane protein necessary for cell adhesion |
title_full | LINKIN, a new transmembrane protein necessary for cell adhesion |
title_fullStr | LINKIN, a new transmembrane protein necessary for cell adhesion |
title_full_unstemmed | LINKIN, a new transmembrane protein necessary for cell adhesion |
title_short | LINKIN, a new transmembrane protein necessary for cell adhesion |
title_sort | linkin a new transmembrane protein necessary for cell adhesion |
topic | human cell cell migration organogenesis cell polarity protein-protein interaction |
url | https://elifesciences.org/articles/04449 |
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