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. 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 ?-propeller structure resembling the ?-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 ?-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.
Mesh Terms:
Amino Acid Sequence, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Adhesion, Cell Membrane, Cell Movement, Conserved Sequence, Gene Deletion, Genes, Helminth, Gonads, HEK293 Cells, Humans, Male, Membrane Proteins, Mitosis, Models, Biological, Molecular Sequence Data, Mutation, Phenotype, Protein Binding, Protein Structure, Tertiary, Protein Transport, RNA Interference
Amino Acid Sequence, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Adhesion, Cell Membrane, Cell Movement, Conserved Sequence, Gene Deletion, Genes, Helminth, Gonads, HEK293 Cells, Humans, Male, Membrane Proteins, Mitosis, Models, Biological, Molecular Sequence Data, Mutation, Phenotype, Protein Binding, Protein Structure, Tertiary, Protein Transport, RNA Interference
Elife
Date: Dec. 01, 2014
PubMed ID: 25437307
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