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dc.contributor.authorOlayioye, Monilola A.-
dc.contributor.authorGraus-Porta, Diana-
dc.contributor.authorBeerli, Roger R.-
dc.contributor.authorRohrer, Jack-
dc.contributor.authorGay, Brigitte-
dc.contributor.authorHynes, Nancy E.-
dc.date.accessioned2018-06-13T08:57:24Z-
dc.date.available2018-06-13T08:57:24Z-
dc.date.issued1998-09-
dc.identifier.issn0270-7306de_CH
dc.identifier.issn1098-5549de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/6818-
dc.description.abstractThe different epidermal growth factor (EGF)-related peptides elicit a diverse array of biological responses as the result of their ability to activate distinct subsets of ErbB receptor dimers, leading to the recruitment of different intracellular signalling networks. To specifically examine dimerization-dependent modulation of receptor signalling, we constructed NIH 3T3 cell lines expressing ErbB-1 and ErbB-2 singly and in pairwise combinations with each other ErbB family member. This model system allowed the comparison of EGF-activated ErbB-1 with ErbB-1 activated by Neu differentiation factor (NDF)-induced heterodimerization with ErbB-4. In both cases, ErbB-1 coupled to the adaptor protein Shc, but only when activated by EGF was it able to interact with Grb2. Compared to the rapid internalization of EGF-activated ErbB-1, NDF-activated ErbB-1 showed delayed internalization characteristics. Furthermore, the p85 subunit of phosphatidylinositol kinase (PI3-K) associated with EGF-activated ErbB-1 in a biphasic manner, whereas association with ErbB-1 transactivated by ErbB-4 was monophasic. The signalling properties of ErbB-2 following heterodimerization with the other ErbB receptors or homodimerization induced by point mutation or monoclonal antibody treatment were also analyzed. ErbB-2 binding to peptides containing the Src homology 2 domain of Grb2 or p85 and the phosphotyrosine binding domain of Shc varied according to the mode of receptor activation. Finally, tryptic phosphopeptide mapping of both ErbB-1 and ErbB-2 revealed that receptor phosphorylation is dependent on the dimerization partner. Differential receptor phosphorylation may, therefore, be the basis for the differences in the signalling properties observed.de_CH
dc.language.isoende_CH
dc.publisherAmerican Society for Microbiologyde_CH
dc.relation.ispartofMolecular and Cellular Biologyde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc571: Physiologie und verwandte Themende_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partnerde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
dc.identifier.doi10.1128/MCB.18.9.5042de_CH
zhaw.funding.euNode_CH
zhaw.issue9de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end5051de_CH
zhaw.pages.start5042de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume18de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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Olayioye, M. A., Graus-Porta, D., Beerli, R. R., Rohrer, J., Gay, B., & Hynes, N. E. (1998). ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner. Molecular and Cellular Biology, 18(9), 5042–5051. https://doi.org/10.1128/MCB.18.9.5042
Olayioye, M.A. et al. (1998) ‘ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner’, Molecular and Cellular Biology, 18(9), pp. 5042–5051. Available at: https://doi.org/10.1128/MCB.18.9.5042.
M. A. Olayioye, D. Graus-Porta, R. R. Beerli, J. Rohrer, B. Gay, and N. E. Hynes, “ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner,” Molecular and Cellular Biology, vol. 18, no. 9, pp. 5042–5051, Sep. 1998, doi: 10.1128/MCB.18.9.5042.
OLAYIOYE, Monilola A., Diana GRAUS-PORTA, Roger R. BEERLI, Jack ROHRER, Brigitte GAY und Nancy E. HYNES, 1998. ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner. Molecular and Cellular Biology. September 1998. Bd. 18, Nr. 9, S. 5042–5051. DOI 10.1128/MCB.18.9.5042
Olayioye, Monilola A., Diana Graus-Porta, Roger R. Beerli, Jack Rohrer, Brigitte Gay, and Nancy E. Hynes. 1998. “ErbB-1 and ErbB-2 Acquire Distinct Signaling Properties Dependent upon Their Dimerization Partner.” Molecular and Cellular Biology 18 (9): 5042–51. https://doi.org/10.1128/MCB.18.9.5042.
Olayioye, Monilola A., et al. “ErbB-1 and ErbB-2 Acquire Distinct Signaling Properties Dependent upon Their Dimerization Partner.” Molecular and Cellular Biology, vol. 18, no. 9, Sept. 1998, pp. 5042–51, https://doi.org/10.1128/MCB.18.9.5042.


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