English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Yrb4p, a yeast Ran–GTP‐binding protein involved in import of ribosomal protein L25 into the nucleus.

Schlenstedt, G., Smirnova, E., Deane, R., Solsbacher, J., Kutay, U., Görlich, D., et al. (1997). Yrb4p, a yeast Ran–GTP‐binding protein involved in import of ribosomal protein L25 into the nucleus. The EMBO Journal, 16(20), 6237-6249. doi:10.1093/emboj/16.20.6237.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3C08-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-0998-1
Genre: Journal Article

Files

show Files
hide Files
:
1922656.pdf (Publisher version), 1MB
Name:
1922656.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://emboj.embopress.org/content/16/20/6237 (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Schlenstedt, G., Author
Smirnova, E., Author
Deane, R., Author
Solsbacher, J., Author
Kutay, U., Author
Görlich, D.1, Author              
Ponstingl, H., Author
Bischoff, F. R., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

Content

show
hide
Free keywords: -
 Abstract: Gsp1p, the essential yeast Ran homologue, is a key regulator of transport across the nuclear pore complex (NPC). We report the identification of Yrb4p, a novel Gsp1p binding protein. The 123 kDa protein was isolated from Saccharomyces cerevisiae cells and found to be related to importin‐β, the mediator of nuclear localization signal (NLS)‐dependent import into the nucleus, and to Pse1p. Like importin‐β, Yrb4p and Pse1p specifically bind to Gsp1p–GTP, protecting it from GTP hydrolysis and nucleotide exchange. The GTPase block of Gsp1p complexed to Yrb4p or Pse1p is released by Yrb1p, which contains a Gsp1p binding domain distinct from that of Yrb4p. This might reflect an in vivo function for Yrb1p. Cells disrupted for YRB4 are defective in nuclear import of ribosomal protein L25, but show no defect in the import of proteins containing classical NLSs. Expression of a Yrb4p mutant deficient in Gsp1p‐binding is dominant‐lethal and blocks bidirectional traffic across the NPC in wild‐type cells. L25 binds to Yrb4p and Pse1p and is released by Gsp1p–GTP. Consistent with its putative role as an import receptor for L25‐like proteins, Yrb4p localizes to the cytoplasm, the nucleoplasm and the NPC.

Details

show
hide
Language(s): eng - English
 Dates: 1997-10-19
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1093/emboj/16.20.6237
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The EMBO Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 16 (20) Sequence Number: - Start / End Page: 6237 - 6249 Identifier: -