Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomes

doi:10.1083/jcb.99.6.2254

This Article

	Full Text (PDF, 1348K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Marcantonio, E. E.
	Articles by Kreibich, G.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Marcantonio, E. E.
	Articles by Kreibich, G.


Social Bookmarking

	What's this?

ARTICLES

Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomes

EE Marcantonio, A Amar-Costesec and G Kreibich

Ribophorins I and II, two transmembrane glycoproteins characteristic of the rough endoplasmic reticulum (ER) are thought to be part of the translocation apparatus for proteins made on membrane bound polysomes. To study the stoichiometry between ribophorins and membrane-bound ribosomes we have determined the RNA and ribophorin content in rat liver microsomes or in microsomal subfractions of different density (i.e., ribosome content). The specificity of antibodies against the ribophorins was demonstrated by Western blot analysis of rat liver rough microsomes separated by 2-dimensional gel electrophoresis. The ribophorin content of microsomal subfractions was determined by indirect immunoprecipitation and for ribophorin I by a radioimmune assay. In the latter assay a molar ratio of ribophorin I/ribosomes approaching one was calculated for total microsomes as well as in the gradient subfractions. We therefore suggest that ribophorins mediate the binding of ribosomes to endoplasmic reticulum membranes or play a role in co-translational process which depend on this binding, such as the insertion of nascent polypeptides into the membrane or their transfer into the cisternal lumen.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Wilson, C. M., Roebuck, Q., High, S. (2008). Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core. Proc. Natl. Acad. Sci. USA 105: 9534-9539 [Abstract] [Full Text]
Sprocati, T., Ronchi, P., Raimondi, A., Francolini, M., Borgese, N. (2006). Dynamic and reversible restructuring of the ER induced by PDMP in cultured cells. J. Cell Sci. 119: 3249-3260 [Abstract] [Full Text]
Kelleher, D. J., Gilmore, R. (2006). An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16: 47R-62R [Abstract] [Full Text]
Ermonval, M., Kitzmuller, C., Mir, A. M., Cacan, R., Ivessa, N. E. (2001). N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation. Glycobiology 11: 565-576 [Abstract] [Full Text]
Prinz, W. A., Grzyb, L., Veenhuis, M., Kahana, J. A., Silver, P. A., Rapoport, T. A. (2000). Mutants Affecting the Structure of the Cortical Endoplasmic Reticulum in Saccharomyces cerevisiae. JCB 150: 461-474 [Abstract] [Full Text]
Fu, J., Kreibich, G. (2000). Retention of Subunits of the Oligosaccharyltransferase Complex in the Endoplasmic Reticulum. J. Biol. Chem. 275: 3984-3990 [Abstract] [Full Text]
de Virgilio, M., Kitzmüller, C., Schwaiger, E., Klein, M., Kreibich, G., Ivessa, N. E. (1999). Degradation of a Short-lived Glycoprotein from the Lumen of the Endoplasmic Reticulum: The Role of N-linked Glycans and the Unfolded Protein Response. Mol. Biol. Cell 10: 4059-4073 [Abstract] [Full Text]
Pizarro-Cerda, J., Meresse, S., Parton, R. G., van der Goot, G., Sola-Landa, A., Lopez-Goni, I., Moreno, E., Gorvel, J.-P. (1998). Brucella abortus Transits through the Autophagic Pathway and Replicates in the Endoplasmic Reticulum of Nonprofessional Phagocytes. Infect. Immun. 66: 5711-5724 [Abstract] [Full Text]
de Virgilio, M., Weninger, H., Ivessa, N. E. (1998). Ubiquitination Is Required for the Retro-translocation of a Short-lived Luminal Endoplasmic Reticulum Glycoprotein to the Cytosol for Degradation by the Proteasome. J. Biol. Chem. 273: 9734-9743 [Abstract] [Full Text]
Ivessa, N. E., Gravotta, D., De Lemos-Chiarandini, C., Kreibich, G. (1997). Functional Protein Prenylation Is Required for the Brefeldin A-dependent Retrograde Transport from the Golgi Apparatus to the Endoplasmic Reticulum. J. Biol. Chem. 272: 20828-20834 [Abstract] [Full Text]
Kelleher, D. J., Gilmore, R. (1997). DAD1, the defender against apoptotic cell death, is a subunit of the mammalian�oligosaccharyltransferase. Proc. Natl. Acad. Sci. USA 94: 4994-4999 [Abstract] [Full Text]
Ivessa, N. E., De Lemos-Chiarandini, C., Gravotta, D., Sabatini, D. D., Kreibich, G. (1995). The Brefeldin A-induced Retrograde Transport from the Golgi Apparatus to the Endoplasmic Reticulum Depends on Calcium Sequestered to Intracellular Stores. J. Biol. Chem. 270: 25960-25967 [Abstract] [Full Text]
Lauring, B., Wang, S., Sakai, H., Davis, T.A., Wiedmann, B., Kreibich, G., Wiedmann, M. (1995). Nascent-polypeptide-associated Complex: A Bridge between Ribosome and Cytosol. Cold Spring Harb Symp Quant Biol 60: 47-56 [Abstract]
Karaoglu, D., Silberstein, S., Kelleher, D.J., Gilmore, R. (1995). The Saccharomyces cerevisiae Oligosaccharyltransferase: A Large Hetero-oligomeric Complex in the Endoplasmic Reticulum. Cold Spring Harb Symp Quant Biol 60: 83-92 [Abstract]
Rajasekaran, A., Morimoto, T, Hanzel, D., Rodriguez-Boulan, E, Kreibich, G (1993). Structural reorganization of the rough endoplasmic reticulum without size expansion accounts for dexamethasone-induced secretory activity in AR42J cells. J. Cell Sci. 105: 333-345 [Abstract]