Document Detail


Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence.
MedLine Citation:
PMID:  3053698     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human asialoglycoprotein receptor H1 is a single-spanning membrane protein with an amino-terminal domain of 40 residues exposed to the cytoplasm and the carboxyl-terminal domain translocated to the exoplasmic side of the membrane. It has been shown earlier that the transmembrane segment functions as an internal uncleaved signal sequence for insertion into the endoplasmic reticulum. In a deletion protein lacking almost the entire cytoplasmic domain, the signal sequence is cleaved at the carboxyl-terminal end of the transmembrane segment. All available criteria suggest that the protein is processed by signal peptidase. The cytoplasmic domain of the receptor does not directly inhibit signal cleavage since it does not detectably hinder cleavage of the normally amino-terminal signal sequence of influenza hemagglutinin in fusion proteins. We suggest that by its size or structure it affects the position of the receptor in the membrane and thus the accessibility of the potential cleavage site to signal peptidase.
Authors:
S R Schmid; M Spiess
Related Documents :
6363408 - Apolipoprotein, an intermediate in the processing of the major lipoprotein of the esche...
23333428 - Fam3b pander and fam3c ilei represent a distinct class of signaling molecules with a no...
11309398 - Distinction between major and minor bacillus signal peptidases based on phylogenetic an...
8076608 - Competition between nuclear localization and secretory signals determines the subcellul...
18606668 - B cells induce tolerance by presenting endogenous peptide-igg on mhc class ii molecules...
16258828 - Heterologous expression of hen egg white lysozyme and resonance assignment of tryptopha...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  263     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1988 Nov 
Date Detail:
Created Date:  1988-12-14     Completed Date:  1988-12-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  16886-91     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Basel, Switzerland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Asialoglycoprotein Receptor
Chromosome Deletion
Endopeptidases / metabolism*
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral / metabolism*
Hexosaminidases / metabolism
Humans
Membrane Proteins*
Molecular Sequence Data
Protein Biosynthesis
Rabbits
Receptors, Immunologic / analysis*
Serine Endopeptidases*
Chemical
Reg. No./Substance:
0/Asialoglycoprotein Receptor; 0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Hemagglutinins, Viral; 0/Membrane Proteins; 0/Receptors, Immunologic; EC 3.2.1.-/Hexosaminidases; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.89/type I signal peptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Primary structure of the lactose permease gene from the yeast Kluyveromyces lactis. Presence of an u...
Next Document:  D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactiv...