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EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues
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 th...
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Formato: | Texto |
Lenguaje: | English |
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2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2970634/ https://www.ncbi.nlm.nih.gov/pubmed/20697431 http://dx.doi.org/10.1038/cr.2010.115 |
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author | Shi, Guanfang Yue, Gang Zhou, Renping |
author_facet | Shi, Guanfang Yue, Gang Zhou, Renping |
author_sort | Shi, Guanfang |
collection | PubMed |
description | 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 phospho-tyrosine 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 293 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. |
format | Text |
id | pubmed-2970634 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
record_format | MEDLINE/PubMed |
spelling | pubmed-29706342011-05-01 EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues Shi, Guanfang Yue, Gang Zhou, Renping Cell Res Article 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 phospho-tyrosine 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 293 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. 2010-08-10 2010-11 /pmc/articles/PMC2970634/ /pubmed/20697431 http://dx.doi.org/10.1038/cr.2010.115 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Shi, Guanfang Yue, Gang Zhou, Renping EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title | EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title_full | EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title_fullStr | EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title_full_unstemmed | EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title_short | EphA3 Functions are Regulated by Collaborating Phosphotyrosine Residues |
title_sort | epha3 functions are regulated by collaborating phosphotyrosine residues |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2970634/ https://www.ncbi.nlm.nih.gov/pubmed/20697431 http://dx.doi.org/10.1038/cr.2010.115 |
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