During collective cell migration, cells establish apicobasal polarity and cell–cell adhesion to allow coordinated movement. By exploiting a gene expression database and Caenorhabditis elegans deletion mutants, Kato et al. identified and characterized LINKIN, a transmembrane protein required for cell–cell adhesion during male gonad collective migration. LINKIN, which localizes to the plasma membrane of all gonadal cells, has an extracellular domain (containing FG–GAP domains) that resembles the ligand-binding domain of α-integrin. As the protein is conserved across metazoans, the authors carried out SILAC in human cells to identify its interactors. Among these, depletion of α-tubulin and the AAA+ ATPases RUVBL1 and RUVBL2 led to similar gonadal defects as lnkn-1 mutants, and these proteins were found to bind to the LINKIN intracellular domain at the plasma membrane. Thus, LINKIN may regulate cell–cell adhesion and microtubule dynamics through these proteins.