English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A.

Aksu, M., Trakhanov, S., & Görlich, D. (2016). Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. Nature Communications, 7: 11952. doi:10.1038/ncomms11952.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-EA25-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-EA46-4
Genre: Journal Article

Files

show Files
hide Files
:
2306550_Suppl_1.pdf (Supplementary material), 9MB
Name:
2306550_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2306550_Suppl_2.pdf (Supplementary material), 786KB
Name:
2306550_Suppl_2.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Aksu, M.1, Author              
Trakhanov, S.1, Author              
Görlich, D.1, Author              
Affiliations:
1Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society, ou_578574              

Content

show
hide
Free keywords: -
 Abstract: Xpo4 is a bidirectional nuclear transport receptor that mediates nuclear export of eIF5A and Smad3 as well as import of Sox2 and SRY. How Xpo4 recognizes such a variety of cargoes is as yet unknown. Here we present the crystal structure of the RanGTP·Xpo4·eIF5A export complex at 3.2 Å resolution. Xpo4 has a similar structure as CRM1, but the NES-binding site is occluded, and a new interaction site evolved that recognizes both globular domains of eIF5A. eIF5A contains hypusine, a unique amino acid with two positive charges, which is essential for cell viability and eIF5A function in translation. The hypusine docks into a deep, acidic pocket of Xpo4 and is thus a critical element of eIF5A’s complex export signature. This further suggests that Xpo4 recognizes other cargoes differently, and illustrates how Xpo4 suppresses – in a chaperone-like manner – undesired interactions of eIF5A inside nuclei.

Details

show
hide
Language(s): eng - English
 Dates: 2016-06-19
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms11952
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 10 Volume / Issue: 7 Sequence Number: 11952 Start / End Page: - Identifier: -