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PMID: 3458708 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminus.

The Journal of cell biology ·Vol. 102 ·No. 6 ·1986-06-00 ·Pages 2169-75

Lipp J, Dobberstein B

Abstract

Invariant (Ii) chain is a membrane-spanning protein that is found associated intracellularly with class II histocompatibility antigens. In the endoplasmic reticulum Ii chain spans the membrane and exposes the NH2 terminus on the cytoplasmic and the COOH terminus on the lumenal side. This orientation across the membrane is demonstrated directly with the monoclonal antibody In-1, which exclusively recognizes the NH2 terminal cytoplasmically exposed part of Ii chain. Membrane insertion of Ii chain requires signal recognition particle and docking protein. When tested in a wheat germ cell free system, signal recognition particle arrests translation of Ii chain. No signal sequence is cleaved from Ii chain upon membrane insertion.

MeSH Terms
Amino Acid Sequence Animals Antibodies, Monoclonal Antigen-Antibody Reactions Cytoplasm/metabolism Histocompatibility Antigens Class II/biosynthesis,immunology,isolation & purification Intracellular Membranes/metabolism Membrane Proteins/immunology,isolation & purification Mice Peptide Fragments/isolation & purification,metabolism Protein Sorting Signals/isolation & purification,metabolism RNA, Messenger/metabolism Spleen
Chemicals
Antibodies, Monoclonal Histocompatibility Antigens Class II Membrane Proteins Peptide Fragments Protein Sorting Signals RNA, Messenger
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lipp J
Dobberstein B
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49 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.102.6.2169
Published
1986-06-00
Pages
2169-75
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2114261
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.102.6.2169 PMC Full Text View journal details
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