English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment

Viegas, A., Yin, D. M., Borggraefe, J., Viennet, T., Falke, M., Schmitz, A., et al. (2020). Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment. Structure, 28: e1-e5, pp. 1-9. doi:10.1016/j.str.2019.11.001.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0005-4764-B Version Permalink: http://hdl.handle.net/21.11116/0000-0005-71E7-7
Genre: Journal Article

Files

show Files
hide Files
:
1-s2.0-S0969212619303855-main.pdf (Preprint), 4MB
 
File Permalink:
-
Name:
1-s2.0-S0969212619303855-main.pdf
Description:
In Press, Corrected Proof
Visibility:
Restricted ( Max Planck Society (every institute); )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
In Press, Corrected Proof

Creators

show
hide
 Creators:
Viegas, Aldino1, Author
Yin, Dongsheng M.2, Author
Borggraefe, Jan1, Author
Viennet, Thibault1, Author
Falke, Marcel1, Author
Schmitz, Anton2, Author
Famulok, Michael2, Author              
Etzkorn, Manuel1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Max Planck Fellow Chemical Biology, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173681              

Content

show
hide
Free keywords: ARNO-Sec7, cytohesins, EGFR, juxtamembrane, NMR
 Abstract: Epidermal growth factor receptors (EGFRs) are central cellular signaling interfaces whose misregulation is related to several severe diseases. Although ligand binding to the extracellular domain is the most obvious regulatory element, also intracellular factors can act as modulators of EGFR activity. The juxtamembrane (JM) segment seems to be the receptor's key interaction interface of these cytoplasmic factors. However, only a limited number of cytoplasmic EGFR modulators are known and a comprehensive understanding of their mode of action is lacking. Here, we report ARNO, a member of the cytohesin family, as another JM-binding protein and structurally characterize the ARNO-EGFR interaction interface. We reveal that its binding mode displays common features and distinct differences with JM's interaction with calmodulin and anionic phospholipids. Furthermore, we show that each interaction can be modulated by additional factors, generating a distinctly regulated network of possible EGFR modulators acting on the intracellular domain of the receptor.

Details

show
hide
Language(s): eng - English
 Dates: 2019-11-252020-01-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2019.11.001
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Abbreviation : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Cell Press
Pages: 14 Volume / Issue: 28 Sequence Number: e1-e5 Start / End Page: 1 - 9 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1