NDLI: A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus.

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A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Foguet, M. Renz, M. Linstedt, A. D. Hauri, H. P. Seelig, H. P. Glick, B. S.
Description	Author Affiliation: Linstedt AD ( Department of Pharmacology, University of Basel, Switzerland.);
Abstract	Unlike conventional membrane proteins of the secretory pathway, proteins anchored to the cytoplasmic surface of membranes by hydrophobic sequences near their C termini follow a posttranslational, signal recognition particle-independent insertion pathway. Many such C-terminally-anchored proteins have restricted intracellular locations, but it is not known whether these proteins are targeted directly to the membranes in which they will ultimately reside. Here we have analyzed the intracellular sorting of the Golgi protein giantin, which consists of a rod-shaped 376-kDa cytoplasmic domain followed by a hydrophobic C-terminal anchor sequence. Unexpectedly, we find that giantin behaves like a conventional secretory protein in that it inserts into the endoplasmic reticulum (ER) and then is transported to the Golgi. A deletion mutant lacking a portion of the cytoplasmic domain adjacent to the membrane anchor still inserts into the ER but fails to reach the Golgi, even though this mutant has a stable folded structure. These findings suggest that the localization of a C-terminally-anchored Golgi protein involves at least three steps: insertion into the ER membrane, controlled incorporation into transport vesicles, and retention within the Golgi.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endoplasmic Reticulum Metabolism Golgi Apparatus Membrane Proteins Protein Processing, Post-Translational Amino Acid Sequence Binding Sites Carcinoma, Hepatocellular Cell Line Ultrastructure Liver Neoplasms Biosynthesis Isolation & Purification Molecular Sequence Data Recombinant Proteins Sequence Deletion Transfection Tumor Cells, Cultured Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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