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Regulation of process retraction and cell migration by Epha3 is mediated by the by the adaptor protein Nck1
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Title
Regulation of process retraction and cell migration by Epha3 is mediated by the by the adaptor protein Nck1
Name
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Hu
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Tianjing
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Tianjing Hu
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(authority = RULIB)
author
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Zhou
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Renping
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Advisory Committee
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Renping Zhou
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chair
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Wagner
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George
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Advisory Committee
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George C Wagner
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(authority = RULIB)
internal member
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Hsu
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Shu
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Advisory Committee
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Shu C Hsu
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(authority = RULIB)
internal member
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Minden
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Audrey
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Advisory Committee
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Audrey Minden
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(authority = RULIB)
outside member
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Rutgers University
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degree grantor
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Graduate School - New Brunswick
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school
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Text
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theses
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2007
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2007
Language
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English
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electronic
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Extent
xiv, 198 pages
Abstract
Members of the largest RTK (receptor tyrosine kinase) family, Eph receptors, and their ligands play pivotal roles in embryonic development. They have been shown to regulate axon guidance, cell migration, tissue boundary formation, synaptogenesis, and angiogenesis. In addition, mis-regulation of the Eph receptor function leads to tumorigenesis and possibly other diseases. However, little is known about signaling pathways downstream of Eph receptors. To shed light on signaling mechanisms of Eph receptors, we conducted a large-scale yeast two-hybrid screen to identify protein that interact with EphA receptors. In this screen, many promising candidates were identified, several of which warrant future investigation. A SH2/SH3 adaptor protein, Nck1, stands out as the strongest interactor with both EphA3 and EphA5. To better understand the signaling mechanisms of the EphAs and the role of Nck1, we performed in-depth studies on fibroblast cells and primary neurons. Here we present evidence that Nck1 interacts directly with activated EphA3 receptor through its SH2 domain and the juxtamembrane domain tyrosine residue 602 on EphA3. We find that the disruption of Nck1 binding by either SH2 domain or SH3 domains negatively regulates EphA3-mediated signaling during cell migration and cell process extension in HEK293A cells. Intriguingly, we also find that expression of Nck1 mutants through adenoviruses is not able to prevent growth cone collapse in primary hippocampal explants. These observations suggest that Nck1 plays a key role in mediating some aspects of EphA receptor functions.
Key words: Eph, ephrin, Receptor tyrosine kinase, SH2 domain, Nck1, Yeast two-hybrid, Hippocampal neuron culture.
Key words: Eph, ephrin, Receptor tyrosine kinase, SH2 domain, Nck1, Yeast two-hybrid, Hippocampal neuron culture.
Note
(type = degree)
Ph.D.
Note
(type = bibliography)
Includes bibliographical references (p. 176-197).
Subject
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Topic
Neuroscience
Subject
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Topic
Receptor-ligand complexes
Subject
(ID = SUBJ3);
(authority = ETD-LCSH)
Topic
Protein-tyrosine kinase
Subject
(ID = SUBJ4);
(authority = ETD-LCSH)
Topic
Central nervous system
Subject
(ID = SUBJ5);
(authority = ETD-LCSH)
Topic
Hippocampus (Brain)
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Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier
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rucore19991600001
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http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.16096
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ETD_563
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NjNbRU
Identifier
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doi:10.7282/T37S7P6T
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ETD doctoral
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Rights
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The author owns the copyright to this work.
Copyright
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Copyright protected
Availability
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Open
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Name
Tianjing Hu
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
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Permission or license
Detail
Non-exclusive ETD license
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Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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