LINKIN, a new transmembrane protein necessary for cell adhesion.

Article Details

Citation

Kato M, Chou TF, Yu CZ, DeModena J, Sternberg PW

LINKIN, a new transmembrane protein necessary for cell adhesion.

Elife. 2014 Dec 1;3:e04449. doi: 10.7554/eLife.04449.

PubMed ID
25437307 [ View in PubMed
]
Abstract

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 beta-propeller structure resembling the alpha-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 alpha-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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
RuvB-like 2Q9Y230Details