Journal
CELL RESEARCH
Volume 20, Issue 11, Pages 1263-1275Publisher
INST BIOCHEMISTRY & CELL BIOLOGY
DOI: 10.1038/cr.2010.115
Keywords
tyrosine phosphorylation; signal transduction; cell migration; growth cone collapse
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Funding
- National Science Foundation (US) [0548541]
- New Jersey Commission on Spinal Cord Research
- NIH [5P01HD023315]
- Division Of Behavioral and Cognitive Sci
- Direct For Social, Behav & Economic Scie [0548541] Funding Source: National Science Foundation
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Ephrin ligands interact with Eph receptors to regulate a wide variety of biological and pathological processes. Recent studies have identified several downstream pathways that mediate the functions of these receptors. Activation of the receptors by ephrin binding results in the phosphorylation of the receptor tyrosine residues. These phosphorylated residues serve as docking sites for many of the downstream signaling pathways. However, the relative contributions of different phosphotyrosine residues remain undefined. In the present study, we mutated each individual tyrosine residues in the cytoplasmic domain of EphA3 receptor and studied the effects using cell migration, process retraction, and growth cone collapse assays. Stimulation of the EphA3 receptor with ephrin-A5 inhibits 293A cell migration, reduces NG108-15 cell neurite outgrowth, and induces growth cone collapse in hippocampal neurons. Mutation of either Y602 or Y779 alone partially decreases EphA3-induced responses. Full abrogation can only be achieved with mutations of both Y602 and Y779. These observations suggest a collaborative model of different downstream pathways.
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