Document Detail

GAS6 mediates adhesion of cells expressing the receptor tyrosine kinase Axl.
MedLine Citation:
PMID:  9287338     Owner:  NLM     Status:  MEDLINE    
Axl is a receptor tyrosine kinase that contains both immunoglobulin and fibronectin III repeats in its extracellular domain reminiscent of cell adhesion molecules. Expression of the receptor tyrosine kinase Axl in the 32D myeloid cell line permits aggregation of cells in response to treatment with the native ligand GAS6; this aggregation was not observed in untreated 32D-Axl cells nor in treated parental cells. This aggregation can be blocked by the addition of excess Axl extracellular domain peptide and does not require intracellular Axl kinase activity. Cell surface binding activity of GAS6 was mapped to distinct plasma membrane interacting domains that are separate from the GAS6 motifs that engage the Axl receptor. This suggests that aggregation is mediated by a heterotypic intercellular mechanism whereby cell-bound GAS6 interacts with Axl receptor on an adjacent cell. This mechanism is supported by our observation that GAS6 binds to 32D parental cells which then permits their aggregation with untreated 32D-Axl cells. We have recently demonstrated that the GAS6-Axl interaction does not initiate mitogenesis in 32D cells. When considered with the adhesion results, these data suggest that an important biological function of the Axl-GAS6 interaction is to mediate cell-cell binding.
P McCloskey; Y W Fridell; E Attar; J Villa; Y Jin; B Varnum; E T Liu
Related Documents :
12912898 - Cf45-1, a secreted protein which participates in dictyostelium group size regulation.
8844408 - Isolation and characterization of a novel cytokinesis-deficient mutant in dictyostelium...
25490748 - Mimulone-induced autophagy through p53-mediated ampk/mtor pathway increases caspase-med...
12535068 - Motility modes of spiroplasma melliferum bc3: a helical, wall-less bacterium driven by ...
2276958 - Acute primary toxoplasmic hepatitis in an adult cat shedding toxoplasma gondii oocysts.
17875648 - Comparison of intra-organellar chaperone capacity for dealing with stress-induced prote...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  272     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1997 Sep 
Date Detail:
Created Date:  1997-10-01     Completed Date:  1997-10-01     Revised Date:  2010-06-02    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  23285-91     Citation Subset:  IM    
Curriculum in Genetics and Molecular Biology, Lineberger Comprehensive Cancer Center at the University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Bone Marrow Cells
Cell Adhesion
Cell Adhesion Molecules / genetics,  metabolism*
Cell Aggregation
Cell Line
Cell Membrane / metabolism
Intercellular Signaling Peptides and Proteins*
Oncogene Proteins / genetics,  metabolism*
Peptide Fragments / genetics,  metabolism
Protein Binding
Proteins / genetics,  metabolism*
Receptor Protein-Tyrosine Kinases / genetics,  metabolism*
Receptors, Cell Surface / genetics,  metabolism*
Recombinant Fusion Proteins / metabolism
Sequence Deletion
Grant Support
Reg. No./Substance:
0/Cell Adhesion Molecules; 0/Intercellular Signaling Peptides and Proteins; 0/Ligands; 0/Oncogene Proteins; 0/Peptide Fragments; 0/Proteins; 0/Receptors, Cell Surface; 0/Recombinant Fusion Proteins; 0/growth arrest-specific protein 6; EC Protein-Tyrosine Kinases; EC receptor tyrosine kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  FAP52, a novel, SH3 domain-containing focal adhesion protein.
Next Document:  The surface region of the bifunctional vaccinia RNA modifying protein VP39 that interfaces with Poly...