Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bpj.2014.03.043
DC FieldValue
dc.titleSpatial organization of epha2 at the cell-cell interface modulates trans-endocytosis of ephrina1
dc.contributor.authorGreene, A.C.
dc.contributor.authorLord, S.J.
dc.contributor.authorTian, A.
dc.contributor.authorRhodes, C.
dc.contributor.authorKai, H.
dc.contributor.authorGroves, J.T.
dc.date.accessioned2016-10-18T06:27:31Z
dc.date.available2016-10-18T06:27:31Z
dc.date.issued2014-05-20
dc.identifier.citationGreene, A.C., Lord, S.J., Tian, A., Rhodes, C., Kai, H., Groves, J.T. (2014-05-20). Spatial organization of epha2 at the cell-cell interface modulates trans-endocytosis of ephrina1. Biophysical Journal 106 (10) : 2196-2205. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bpj.2014.03.043
dc.identifier.issn15420086
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/128541
dc.description.abstractEphA2 is a receptor tyrosine kinase (RTK) that is sensitive to spatial and mechanical aspects of the cell's microenvironment. Misregulation of EphA2 occurs in many aggressive cancers. Although its juxtacrine signaling geometry (EphA2's cognate ligand ephrinA1 is expressed on the surface of an apposing cell) provides a mechanism by which the receptor may experience extracellular forces, this also renders the system challenging to decode. By depositing living cells on synthetic supported lipid membranes displaying ephrinA1, we have reconstituted key features of the juxtacrine EphA2-ephrinA1 signaling system while maintaining the ability to perturb the spatial and mechanical properties of the membrane-cell interface with precision. In addition, we developed a trans-endocytosis assay to monitor internalization of ephrinA1 from a supported membrane into the apposing cell using a quantitative three-dimensional fluorescence microscopy assay. Using this experimental platform to mimic a cell-cell junction, we found that the signaling complex is not efficiently internalized when lateral reorganization at the membrane-cell contact sites is physically hindered. This suggests that EphA2-ephrinA1 trans-endocytosis is sensitive to the mechanical properties of a cell's microenvironment and may have implications in physical aspects of tumor biology. © 2014 Biophysical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bpj.2014.03.043
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1016/j.bpj.2014.03.043
dc.description.sourcetitleBiophysical Journal
dc.description.volume106
dc.description.issue10
dc.description.page2196-2205
dc.description.codenBIOJA
dc.identifier.isiut000336353200014
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

28
checked on Nov 26, 2020

WEB OF SCIENCETM
Citations

27
checked on Nov 26, 2020

Page view(s)

63
checked on Nov 28, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.