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The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 α3 chain is crucial for integrin α3β1 binding and cell adhesion

Cited 66 time in Web of Science Cited 65 time in Scopus
Authors
Min, Byung-Moo; Kim, Jin-Man; Park, Won Ho
Issue Date
2005-03
Publisher
Elsevier
Citation
Experimental Cell Research 304 (2005) 317-327
Keywords
Laminin-5Novel motif PPFLMLLKGSTRCell behaviorIntegrin α3β1FAK signaling
Abstract
Laminin-5 regulates various cellular functions, including cell adhesion, spreading, and motility. Here, we expressed the five human laminin α3 chain globular (LG) domains as monomeric, soluble fusion proteins, and examined their biological functions and signaling. Recombinant LG3 (rLG3) protein, unlike rLG1, rLG2, rLG4, and rLG5, played roles in cell adhesion, spreading, and integrin α3β1 binding. More significantly, we identified a novel motif (PPFLMLLKGSTR) in the LG3 domain that is crucial for these responses. Studies with the synthetic peptides delineated the PPFLMLLKGSTR peptide within LG3 domain as a major site for both integrin α3β1 binding and cell adhesion. Substitution mutation experiments suggest that the Arg residue is important for these activities. rLG3 protein- and PPFLMLLKGSTR peptide-induced keratinocyte adhesion triggered cell signaling through FAK phosphorylation at tyrosine-397 and -577. To our knowledge, this is the first report demonstrating that the PPFLMLLKGSTR peptide within the LG3 domain is a novel motif that is capable of supporting integrin α3β1-dependent cell adhesion and spreading.
ISSN
0014-4827
Language
English
URI
https://hdl.handle.net/10371/69709
DOI
https://doi.org/10.1016/j.yexcr.2004.11.009
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College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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