JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Porat, A.
Right arrow Articles by Elazar, Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Porat, A.
Right arrow Articles by Elazar, Z.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 19, 14457-14465, May 12, 2000

A 56-kDa Selenium-binding Protein Participates in Intra-Golgi Protein Transport*

Amir Porat, Yuval Sagiv, and Zvulun ElazarDagger

From the Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel

Transport of proteins between intracellular membrane compartments is a highly regulated process that depends on several cytosolic factors. By using the well characterized intra-Golgi cell-free transport assay, we purified from bovine brain cytosol a 56-kDa protein that shows a significant transport activity. Partial sequencing of four tryptic peptides obtained from the 56-kDa protein revealed its identity to a cytosolic protein previously characterized as a selenium-binding protein, SBP56. Recombinant SBP56 expressed in Escherichia coli exhibited transport activity when added to the cell-free intra-Golgi transport. Affinity purified anti-SBP56 polyclonal antibodies specifically inhibited intra-Golgi transport in vitro. Although SBP56 is predominantly localized in the cytosol, a significant amount is associated with membranes. Subcellular fractionation showed that this protein is peripherally associated with the Golgi membrane. The experiments presented in this study indicate that SBP56 participates in late stages of intra-Golgi protein transport.

* This work was supported in part by the German-Israeli Foundation and the Weizmann Institute Minerva Center.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Incumbent of the Shloimo and Michla Tomarin Career Development Chair of Membrane Physiology. To whom correspondence should be addressed: Dept. of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: 972-8-9343682; Fax: 972-8-9344112; E-mail: bmzevi@wicc.weizmann.ac.il.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
C. Dutilleul, A. Jourdain, J. Bourguignon, and V. Hugouvieux
The Arabidopsis Putative Selenium-Binding Protein Family: Expression Study and Characterization of SBP1 as a Potential New Player in Cadmium Detoxification Processes
Plant Physiology, May 1, 2008; 147(1): 239 - 251.
[Abstract] [Full Text] [PDF]

Home page
 J DAIRY SCIHome page
K. M. Daniels, K. E. Webb Jr., M. L. McGilliard, M. J. Meyer, M. E. Van Amburgh, and R. M. Akers
Effects of body weight and nutrition on mammary protein expression profiles in Holstein heifers.
J Dairy Sci, November 1, 2006; 89(11): 4276 - 4288.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
R. Pastorelli, D. Carpi, R. Campagna, L. Airoldi, R. Pohjanvirta, M. Viluksela, H. Hakansson, P. C. Boutros, I. D. Moffat, A. B. Okey, et al.
Differential Expression Profiling of the Hepatic Proteome in a Rat Model of Dioxin Resistance: CORRELATION WITH GENOMIC AND TRANSCRIPTOMIC ANALYSES
Mol. Cell. Proteomics, May 1, 2006; 5(5): 882 - 894.
[Abstract] [Full Text] [PDF]

Home page
 Endocr. Rev.Home page
J. Kohrle, F. Jakob, B. Contempre, and J. E. Dumont
Selenium, the Thyroid, and the Endocrine System
Endocr. Rev., December 1, 2005; 26(7): 944 - 984.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Respir. Cell Mol. Bio.Home page
A. M. Wheelock, B. C. Boland, M. Isbell, D. Morin, T. C. Wegesser, C. G. Plopper, and A. R. Buckpitt
In Vivo Effects of Ozone Exposure on Protein Adduct Formation by 1-Nitronaphthalene in Rat Lung
Am. J. Respir. Cell Mol. Biol., August 1, 2005; 33(2): 130 - 137.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Stuven, A. Porat, F. Shimron, E. Fass, D. Kaloyanova, B. Brugger, F. T. Wieland, Z. Elazar, and J. B. Helms
Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane
J. Biol. Chem., December 26, 2003; 278(52): 53112 - 53122.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Porat and Z. Elazar
Regulation of Intra-Golgi Membrane Transport by Calcium
J. Biol. Chem., September 15, 2000; 275(38): 29233 - 29237.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Teo, L. Tan, L. Lim, and E. Manser
The Tyrosine Kinase ACK1 Associates with Clathrin-coated Vesicles through a Binding Motif Shared by Arrestin and Other Adaptors
J. Biol. Chem., May 18, 2001; 276(21): 18392 - 18398.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.