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PMID: 3396535 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Binding to membrane proteins within the endoplasmic reticulum cannot explain the retention of the glucose-regulated protein GRP78 in Xenopus oocytes.

The EMBO journal ·Vol. 7 ·No. 3 ·1988-03-00 ·Pages 633-8

Ceriotti A, Colman A

Abstract

We have studied the compartmentation and movement of the rat 78-kd glucose-regulated protein (GRP78) and other secretory and membrane proteins in Xenopus oocytes. Full length GRP78, normally found in the lumen of rat endoplasmic reticulum (ER), is localized to a membraneous compartment in oocytes and is not secreted. A truncated GRP78 lacking the C-terminal (KDEL) ER retention signal is secreted, although at a slow rate. When the synthesis of radioactive GRP78 is confined to a polar (animal or vegetal) region of the oocyte and the subsequent movement across the oocyte monitored, we find that both full-length and truncated GRP78 move at similar rates and only slightly slower than a secretory protein, chick ovalbumin. In contrast, a plasma membrane protein (influenza haemagglutinin) and two ER membrane proteins (rotavirus VP10 and a mutant haemagglutinin) remained confined to their site of synthesis. We conclude that the retention of GRP78 in the ER is not due to its tight binding to a membrane-bound receptor.

MeSH Terms
Animals Endoplasmic Reticulum/metabolism HSP70 Heat-Shock Proteins Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral/metabolism Membrane Proteins/metabolism Oocytes/metabolism Protein Processing, Post-Translational RNA, Messenger/metabolism Time Factors Xenopus laevis
Chemicals
HSP70 Heat-Shock Proteins Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral Membrane Proteins RNA, Messenger glucose-regulated proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ceriotti A
Department of Biological Sciences, University of Warwick, Coventry, UK.
Colman A
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33 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1988-03-00
Pages
633-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC454367
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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