N-glycosylation of the I-like domain of beta1 integrin is essential for beta1 integrin expression and biological function: identification of the minimal N-glycosylation requirement for alpha5beta1.

ABSTRACT: N-Glycosylation of integrin alpha5beta1 plays a crucial role in cell spreading, cell migration, ligand binding, and dimer formation, but the detailed mechanisms by which N-glycosylation mediates these functions remain unclear. In a previous study, we showed that three potential N-glycosylation sites (alpha5S3-5) on the beta-propeller of the alpha5 subunit are essential to the functional expression of the subunit. In particular, site 5 (alpha5S5) is the most important for its expression on the cell surface. In this study, the function of the N-glycans on the integrin beta1 subunit was investigated using sequential site-directed mutagenesis to remove the combined putative N-glycosylation sites. Removal of the N-glycosylation sites on the I-like domain of the beta1 subunit (i.e. the Delta4-6

SUBMITTER: Isaji T 

PROVIDER: S-EPMC2673289 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature