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A dual role for COOH-terminal lysine residues in pre-Golgi retention and endocytosis of ERGIC-53
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 153388
Author(s) Kappeler, F; Itin, C; Schindler, R; Hauri, H P
Author(s) at UniBasel Hauri, Hans-Peter
Year 1994
Title A dual role for COOH-terminal lysine residues in pre-Golgi retention and endocytosis of ERGIC-53
Journal Journal of biological chemistry
Volume 269
Number 9
Pages / Article-Number 6279-81
Keywords Amino Acid Sequence; Animals; Cell Line; DNA; Complementary/metabolism; *Endocytosis; Endoplasmic Reticulum/*metabolism; Fluorescent Antibody Technique; Golgi Apparatus/*metabolism; Kinetics; *Lysine; *Mannose-Binding Lectins; Membrane Proteins/biosynthesis/chemistry/*metabolism; Molecular Sequence Data; Serine; Transfection
Abstract ERGIC-53 (former designation, p53) is a 53-kDa nonglycosylated, dimeric, and hexameric type I membrane protein that has been established as a marker protein for a tubulovesicular intermediate compartment in which protein transport from the endoplasmic reticulum to the Golgi apparatus is blocked at 15 degrees C. Although ERGIC-53 is not a resident protein of the rough endoplasmic reticulum its cDNA sequence carries a double lysine endoplasmic reticulum retention motif at the cytoplasmically exposed COOH terminus. Here we report that overexpression of ERGIC-53 in COS cells saturates its intracellular retention system leading to the appearance of ERGIC-53 at the cell surface. Cell surface ERGIC-53 is efficiently endocytosed by a mechanism that is disturbed when the two critical lysines of the endoplasmic reticulum retention motif are replaced by serines. The results suggest a mechanistic similarity of pre-Golgi retention by the double lysine motif and lysine-based endocytosis.
Publisher American Society of Biological Chemists
ISSN/ISBN 0021-9258
edoc-URL http://edoc.unibas.ch/dok/A5257791
Full Text on edoc No
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/8119975
ISI-Number WOS:A1994MZ50300006
Document type (ISI) Journal Article
 
   

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