NDLI: Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome

Content Provider	PubMed Central
Author	Hughes, Eric A. Hammond, Craig Cresswell, Peter
Copyright Year	1997
Abstract	N-acetyl-l-leucyl-l-leucyl-l-norleucinal (LLnL), which reversibly inhibits the proteasome in addition to other proteases, and a more specific irreversible inhibitor of the proteasome, lactacystin, were found to cause the accumulation of major histocompatibility complex (MHC) class I heavy chains in the cytosol of the β2-microglobulin-deficient cell line Daudi and the TAP-deficient cell line .174. These cell lines, which are severely impaired in their ability to fold MHC class I heavy chain, showed an accumulation of soluble class I heavy chains at different rates over a period of hours in the presence of LLnL. The accumulation of soluble class I heavy chains in the presence of either LLnL or lactacystin was easily revealed in Daudi and .174 but almost undetectable in a Daudi transfectant expressing β2-microglobulin and in 45.1, the wild-type parent of .174. The soluble class I heavy chain was also found to be devoid of its N-linked glycan and to be located in the cytosol. When the gene for ICP47, a herpes simplex virus protein that blocks the translocation of peptides into the endoplasmic reticulum, was transfected into 45.1, a similar accumulation of soluble MHC class I heavy chain was detectable. These data suggest that in cells where the MHC class I molecule is unable to assemble properly, the misfolded heavy chain is removed from the endoplasmic reticulum to the cytosol, deglycosylated, and degraded by the proteasome.
Starting Page	1896
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-03-04
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome.

Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains.

Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex.

Human cytomegalovirus US2 destabilizes major histocompatibility complex class I heavy chains.

Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum

Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition

Peptide influences the folding and intracellular transport of free major histocompatibility complex class I heavy chains

Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic epitope borne by class I major histocompatibility complex heavy chains

Major Histocompatibility Complex class I heavy chains localize in both cytoplasmic and nuclear compartment

Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome

Similar Documents

Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome.

Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains.

Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex.

Human cytomegalovirus US2 destabilizes major histocompatibility complex class I heavy chains.

Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum

Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition

Peptide influences the folding and intracellular transport of free major histocompatibility complex class I heavy chains

Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic epitope borne by class I major histocompatibility complex heavy chains

Major Histocompatibility Complex class I heavy chains localize in both cytoplasmic and nuclear compartment

Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome