Unknown

Dataset Information

0

JAM-A interacts with α3β1 integrin and tetraspanins CD151 and CD9 to regulate collective cell migration of polarized epithelial cells.


ABSTRACT: Junctional adhesion molecule (JAM)-A is a cell adhesion receptor localized at epithelial cell-cell contacts with enrichment at the tight junctions. Its role during cell-cell contact formation and epithelial barrier formation has intensively been studied. In contrast, its role during collective cell migration is largely unexplored. Here, we show that JAM-A regulates collective cell migration of polarized epithelial cells. Depletion of JAM-A in MDCK cells enhances the motility of singly migrating cells but reduces cell motility of cells embedded in a collective by impairing the dynamics of cryptic lamellipodia formation. This activity of JAM-A is observed in cells grown on laminin and collagen-I but not on fibronectin or vitronectin. Accordingly, we find that JAM-A exists in a complex with the laminin- and collagen-I-binding α3β1 integrin. We also find that JAM-A interacts with tetraspanins CD151 and CD9, which both interact with α3β1 integrin and regulate α3β1 integrin activity in different contexts. Mapping experiments indicate that JAM-A associates with α3β1 integrin and tetraspanins CD151 and CD9 through its extracellular domain. Similar to depletion of JAM-A, depletion of either α3β1 integrin or tetraspanins CD151 and CD9 in MDCK cells slows down collective cell migration. Our findings suggest that JAM-A exists with α3β1 integrin and tetraspanins CD151 and CD9 in a functional complex to regulate collective cell migration of polarized epithelial cells.

SUBMITTER: Tholmann S 

PROVIDER: S-EPMC8784505 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC4630866 | biostudies-literature
| S-EPMC2488315 | biostudies-literature
| S-EPMC3629153 | biostudies-literature
| S-EPMC3844903 | biostudies-literature
| S-EPMC8191020 | biostudies-literature
| S-EPMC4322965 | biostudies-literature
| S-EPMC3525767 | biostudies-literature
| S-EPMC4846106 | biostudies-literature
| S-EPMC164635 | biostudies-literature
| S-EPMC3383836 | biostudies-literature