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dc.contributor.authorWang, Yue
dc.contributor.authorShang, Yuan
dc.contributor.authorLi, Jianchao
dc.contributor.authorChen, Weidi
dc.contributor.authorLi, Gang
dc.contributor.authorWan, Jun
dc.contributor.authorLiu, Wei
dc.contributor.authorZhang, Mingjie
dc.date.accessioned2018-08-31T19:26:01Z
dc.date.available2018-08-31T19:26:01Z
dc.date.issued2018-05-11
dc.identifier.citationeLife 2018;7:e35677en_US
dc.identifier.issn2050-084X
dc.identifier.pmid29749928
dc.identifier.doi10.7554/eLife.35677
dc.identifier.doi10.7554/eLife.35677.001
dc.identifier.doi10.7554/eLife.35677.002
dc.identifier.doi10.7554/eLife.35677.003
dc.identifier.doi10.7554/eLife.35677.004
dc.identifier.doi10.7554/eLife.35677.005
dc.identifier.doi10.7554/eLife.35677.006
dc.identifier.doi10.7554/eLife.35677.007
dc.identifier.doi10.7554/eLife.35677.008
dc.identifier.doi10.7554/eLife.35677.009
dc.identifier.doi10.7554/eLife.35677.010
dc.identifier.doi10.7554/eLife.35677.011
dc.identifier.doi10.7554/eLife.35677.012
dc.identifier.doi10.7554/eLife.35677.013
dc.identifier.doi10.7554/eLife.35677.014
dc.identifier.doi10.7554/eLife.35677.015
dc.identifier.doi10.7554/eLife.35677.016
dc.identifier.doi10.7554/eLife.35677.017
dc.identifier.doi10.7554/eLife.35677.029
dc.identifier.doi10.7554/eLife.35677.030
dc.identifier.doi10.7554/eLife.35677.019
dc.identifier.doi10.7554/eLife.35677.020
dc.identifier.urihttp://hdl.handle.net/10150/628620
dc.description.abstractThe Eph receptor tyrosine kinase (RTK) family is the largest subfamily of RTKs playing critical roles in many developmental processes such as tissue patterning, neurogenesis and neuronal circuit formation, angiogenesis, etc. How the 14 Eph proteins, via their highly similar cytoplasmic domains, can transmit diverse and sometimes opposite cellular signals upon engaging ephrins is a major unresolved question. Here, we systematically investigated the bindings of each SAM domain of Eph receptors to the SAM domains from SHIP2 and Odin, and uncover a highly specific SAM SAM interaction-mediated cytoplasmic Eph-effector binding pattern. Comparative X-ray crystallographic studies of several SAM SAM heterodimer complexes, together with biochemical and cell biology experiments, not only revealed the exquisite specificity code governing Eph/effector interactions but also allowed us to identify SAMD5 as a new Eph binding partner. Finally, these Eph/effector SAM heterodimer structures can explain many Eph SAM mutations identified in patients suffering from cancers and other diseases.en_US
dc.description.sponsorshipMinistry of Science and Technology [2014CB910204, 2016YFA0501903]; Natural Science Foundation of Guangdong Province [2016A030312016]; Shenzhen Basic Research Grant, Shenzhen, China [JCYJ20160229153100269, JCYJ20160427185712266, JCYJ20170411090807530]; National Natural Science Foundation of China [31670765]; Asia Fund for Cancer Research [AFCR17SC01]en_US
dc.language.isoenen_US
dc.publisherELIFE SCIENCES PUBLICATIONS LTDen_US
dc.relation.urlhttps://elifesciences.org/articles/35677en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#abstracten_US
dc.relation.urlhttps://elifesciences.org/articles/35677#digesten_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#table1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig2en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig2s1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig2s2en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig2s3en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig2s4en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig2s5en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig3en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig3s1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#fig3s2en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig4en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig5en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#fig6en_US
dc.relation.urlhttps://elifesciences.org/articles/35677/figures#transrepformen_US
dc.relation.urlhttps://elifesciences.org/articles/35677#SA1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#SA2en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#respfig1en_US
dc.relation.urlhttps://elifesciences.org/articles/35677#respfig2en_US
dc.rights© 2018, Wang et al. This article is distributed under the terms of the Creative Commons Attribution License.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleSpecific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactionsen_US
dc.typeArticleen_US
dc.contributor.departmentUniv Arizona, Ctr Biomed Informat & Biostaten_US
dc.identifier.journalELIFEen_US
dc.description.noteOpen Access Journal*/Paid Open Access after January 2017*en_US
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.en_US
dc.eprint.versionFinal published versionen_US
dc.source.journaltitleeLife
dc.source.volume7
refterms.dateFOA2018-08-31T19:26:02Z


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© 2018, Wang et al. This article is distributed under the terms of the Creative Commons Attribution License.
Except where otherwise noted, this item's license is described as © 2018, Wang et al. This article is distributed under the terms of the Creative Commons Attribution License.