| First Author | Elder BH | Year | 2016 |
| Journal | Biochem Biophys Res Commun | Volume | 478 |
| Issue | 3 | Pages | 1248-53 |
| PubMed ID | 27553271 | Mgi Jnum | J:239030 |
| Mgi Id | MGI:5824792 | Doi | 10.1016/j.bbrc.2016.08.102 |
| Citation | Elder BH, et al. (2016) Mouse fibroblasts null for the long isoform of beta1,4-galactosyltransferase-I show defective cell-matrix interactions. Biochem Biophys Res Commun 478(3):1248-53 |
| abstractText | beta1,4 Galactosyltransferase-I (GalT-I) is expressed as two nearly identical polypeptides that differ only in the length of their cytoplasmic domains. The longer isoform has been implicated as a cell surface receptor for extracellular glycoside ligands, such as laminin. To more stringently test the function of the long GalT-I isoform during cell interactions with laminin, we created multiple independent fibroblastic cell lines that fail to express the long isoform, but which express the short GalT-I isoform normally and appear to have normal intracellular galactosylation. Cells devoid of the long GalT-I isoform are unable to adhere and spread on laminin substrates as well as control cells, but retain near normal interactions with fibronectin, which do not rely upon surface GalT-I function. The loss of the long GalT-I isoform also leads to a loss of actin stress fibers, focal adhesions and rac GTPase activation. |
