<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>180(6)</volume><submitter>Goetz JG</submitter><pubmed_abstract>Both tyrosine-phosphorylated caveolin-1 (pY14Cav1) and GlcNAc-transferase V (Mgat5) are linked with focal adhesions (FAs); however, their function in this context is unknown. Here, we show that galectin-3 binding to Mgat5-modified N-glycans functions together with pY14Cav1 to stabilize focal adhesion kinase (FAK) within FAs, and thereby promotes FA disassembly and turnover. Expression of the Mgat5/galectin lattice alone induces FAs and cell spreading. However, FAK stabilization in FAs also requires expression of pY14Cav1. In cells lacking the Mgat5/galectin lattice, pY14Cav1 is not sufficient to promote FAK stabilization, FA disassembly, and turnover. In human MDA-435 cancer cells, Cav1 expression, but not mutant Y14FCav1, stabilizes FAK exchange and stimulates de novo FA formation in prot</pubmed_abstract><journal>The Journal of cell biology</journal><pagination>1261-75</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2290850</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1.</pubmed_title><pmcid>PMC2290850</pmcid><pubmed_authors>Goetz JG</pubmed_authors><pubmed_authors>Lajoie P</pubmed_authors><pubmed_authors>Kojic LD</pubmed_authors><pubmed_authors>Scudamore T</pubmed_authors><pubmed_authors>Joshi B</pubmed_authors><pubmed_authors>Strugnell SS</pubmed_authors><pubmed_authors>Nabi IR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1.</name><description>Both tyrosine-phosphorylated caveolin-1 (pY14Cav1) and GlcNAc-transferase V (Mgat5) are linked with focal adhesions (FAs); however, their function in this context is unknown. Here, we show that galectin-3 binding to Mgat5-modified N-glycans functions together with pY14Cav1 to stabilize focal adhesion kinase (FAK) within FAs, and thereby promotes FA disassembly and turnover. Expression of the Mgat5/galectin lattice alone induces FAs and cell spreading. However, FAK stabilization in FAs also requires expression of pY14Cav1. In cells lacking the Mgat5/galectin lattice, pY14Cav1 is not sufficient to promote FAK stabilization, FA disassembly, and turnover. In human MDA-435 cancer cells, Cav1 expression, but not mutant Y14FCav1, stabilizes FAK exchange and stimulates de novo FA formation in prot</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Mar</publication><modification>2025-04-22T07:06:07.865Z</modification><creation>2019-03-26T23:20:00Z</creation></dates><accession>S-EPMC2290850</accession><cross_references><pubmed>18347068</pubmed><doi>10.1083/jcb.200709019</doi></cross_references></HashMap>