Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides

doi:10.1083/jcb.111.4.1335

This Article

	Full Text (PDF, 1269K)
	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 Yu, Y. H.
	Articles by Kreibich, G.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Yu, Y. H.
	Articles by Kreibich, G.


Social Bookmarking

	What's this?

ARTICLES

Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides

YH Yu, DD Sabatini and G Kreibich
Department of Cell Biology, New York University School of Medicine, New York 10016.

Polyclonal antibodies directed against ribophorins I and II, two membrane glycoproteins characteristic of the rough endoplasmic reticulum, inhibit the cotranslational translocation of a secretory protein growth hormone into the lumen of dog pancreas or rat liver microsomes. As expected, site-specific antibodies to epitopes located within the cytoplasmic domain of ribophorin I, but not antibodies to epitopes in the luminal domain of this protein, were effective in inhibiting translocation. Since monovalent Fab fragments were as inhibitory as intact IgG molecules, ribophorins must be closely associated with the translocation site and, therefore, are likely to function at some stage in the translocation process. In all cases, the antibodies that inhibited translocation also caused a significant reduction in total protein synthesis and treatments that neutralized their capacity to inhibit translocation also prevented their inhibitory effect on protein synthesis. This would be expected if the antibodies blocked the membrane-mediated relief of the SRP-induced arrest of polypeptide elongation. The antibodies were effective only when added before translocation was allowed to begin. In this case, they prevented the targeting of active ribosomes containing mRNA and nascent chains to the ER membrane. Thus, ribophorins must either directly participate in targeting or be so close to the targeting site that the antibodies sterically blocked this early phase of the translocation process.
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:

Ge, X., Loh, H. H., Law, P.-Y. (2009). {micro}-Opioid Receptor Cell Surface Expression Is Regulated by Its Direct Interaction with Ribophorin I. Mol. Pharmacol. 75: 1307-1316 [Abstract] [Full Text]
Kelleher, D. J., Gilmore, R. (2006). An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16: 47R-62R [Abstract] [Full Text]
Chavan, M., Yan, A., Lennarz, W. J. (2005). Subunits of the Translocon Interact with Components of the Oligosaccharyl Transferase Complex. J. Biol. Chem. 280: 22917-22924 [Abstract] [Full Text]
Nilsson, I., Kelleher, D. J., Miao, Y., Shao, Y., Kreibich, G., Gilmore, R., von Heijne, G., Johnson, A. E. (2003). Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex. JCB 161: 715-725 [Abstract] [Full Text]
Nikonov, A. V., Snapp, E., Lippincott-Schwartz, J., Kreibich, G. (2002). Active translocon complexes labeled with GFP-Dad1 diffuse slowly as large polysome arrays in the endoplasmic reticulum. JCB 158: 497-506 [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]
Pedrazzini, E., Villa, A., Longhi, R., Bulbarelli, A., Borgese, N. (2000). Mechanism of Residence of Cytochrome B(5), a Tail-Anchored Protein, in the Endoplasmic Reticulum. JCB 148: 899-914 [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]
Sanjay, A., Fu, J., Kreibich, G. (1998). DAD1 Is Required for the Function and the Structural Integrity of the Oligosaccharyltransferase Complex. J. Biol. Chem. 273: 26094-26099 [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]
Fu, J., Ren, M., Kreibich, G. (1997). Interactions among Subunits of the Oligosaccharyltransferase Complex. J. Biol. Chem. 272: 29687-29692 [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]
Wiest, D. L., Bhandoola, A., Punt, J., Kreibich, G., McKean, D., Singer, A. (1997). Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular�chaperones. Proc. Natl. Acad. Sci. USA 94: 1884-1889 [Abstract] [Full Text]
Yang, M., Ellenberg, J., Bonifacino, J. S., Weissman, A. M. (1997). The Transmembrane Domain of a Carboxyl-terminal Anchored Protein Determines Localization to the Endoplasmic Reticulum. J. Biol. Chem. 272: 1970-1975 [Abstract] [Full Text]
Seiser, C., Posch, M., Thompson, N., K�hn, L. C. (1995). Effect of Transcription Inhibitors on the Iron-dependent Degradation of Transferrin Receptor mRNA. J. Biol. Chem. 270: 29400-29406 [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]
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]