NDLI: Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum.

Please wait, while we are loading the content...

Year: 2016, Volume: 35

Year: 2015, Volume: 34

Year: 2014, Volume: 33

Year: 2013, Volume: 33

Year: 2013, Volume: 32

Year: 2012, Volume: 32

Year: 2012, Volume: 31

Year: 2011, Volume: 30

Year: 2010, Volume: 29

Year: 2009, Volume: 28

Year: 2008, Volume: 27

Year: 2007, Volume: 26

Year: 2006, Volume: 26

Year: 2006, Volume: 25

Year: 2005, Volume: 24

Year: 2004, Volume: 24

Year: 2004, Volume: 23

Year: 2003, Volume: 22

Year: 2002, Volume: 21

Year: 2001, Volume: 20

Year: 2000, Volume: 19

Year: 1999, Volume: 18

Year: 1998, Volume: 17

Year: 1997, Volume: 16

Year: 1996, Volume: 15

Year: 1995, Volume: 14

Year: 1994, Volume: 13

Year: 1993, Volume: 12

Year: 1992, Volume: 11

Year: 1991, Volume: 10

Year: 1991, Volume: 10, Issue: 13

Year: 1991, Volume: 10, Issue: 12

Year: 1991, Volume: 10, Issue: 11

Year: 1991, Volume: 10, Issue: 10

Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure.

Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease.

A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei: lipid structure and biosynthesis.

Sm25, a major schistosome tegumental glycoprotein, is dependent on palmitic acid for membrane attachment.

Theoretical and functional analysis of the SIV fusion peptide.

Electrostatic destabilization of the cytochrome b6f complex in the thylakoid membrane.

Protein targeting towards the thylakoid lumen of chloroplasts: proper localization of fusion proteins is only observed in vivo.

Decoding signals for membrane protein assembly using alkaline phosphatase fusions.

Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum.

A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes.

Cloning, expression, pharmacology and regulation of a delayed rectifier K+ channel in mouse heart.

Novel genes for potential ligand-binding proteins in subregions of the olfactory mucosa.

A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types.

Identification of the second subunit of the murine interleukin-5 receptor: interleukin-3 receptor-like protein, AIC2B is a component of the high affinity interleukin-5 receptor.

Leukemia inhibitory factor receptor is structurally related to the IL-6 signal transducer, gp130.

Ligand-induced transphosphorylation between different FGF receptors.

Functional domains of the granulocyte colony-stimulating factor receptor.

Scatter factor and hepatocyte growth factor are indistinguishable ligands for the MET receptor.

p53 is frequently mutated in Burkitt's lymphoma cell lines.

The plant oncogene rolC is responsible for the release of cytokinins from glucoside conjugates.

The GTPase stimulatory activities of the neurofibromatosis type 1 and the yeast IRA2 proteins are inhibited by arachidonic acid.

The tcl-3 proto-oncogene altered by chromosomal translocation in T-cell leukemia codes for a homeobox protein.

The ltk gene encodes a novel receptor-type protein tyrosine kinase.

Casein kinase II induces c-fos expression via the serum response element pathway and p67SRF phosphorylation in living fibroblasts.

Several different upstream promoter elements can potentiate transactivation by the BPV-1 E2 protein.

Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus.

Analysis of the Rhodobacter capsulatus puc operon: the pucC gene plays a central role in the regulation of LHII (B800-850 complex) expression.

Different mechanisms regulate muscle-specific AChR gamma- and epsilon-subunit gene expression.

Transcriptional activation by heterodimers of the achaete-scute and daughterless gene products of Drosophila.

The Drosophila neurogenic gene neuralized encodes a novel protein and is expressed in precursors of larval and adult neurons.

Effects of retinoic acid excess on expression of Hox-2.9 and Krox-20 and on morphological segmentation in the hindbrain of mouse embryos.

The oct3 gene, a gene for an embryonic transcription factor, is controlled by a retinoic acid repressible enhancer.

POU proteins bend DNA via the POU-specific domain.

A negatively acting DNA sequence element mediates phytochrome-directed repression of phyA gene transcription.

A novel switch-activating site (SAS1) and its cognate binding factor (SAP1) required for efficient mat1 switching in Schizosaccharomyces pombe.

Nucleosomes are positioned with base pair precision adjacent to the alpha 2 operator in Saccharomyces cerevisiae.

DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: involvement of protein phosphorylation in nucleosome spacing.

Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome.

Expression of the replication protein Arp of phasyl shows dual regulation by an antisense promoter.

In vitro deadenylation of mammalian mRNA by a HeLa cell 3' exonuclease.

Transfer of rpl22 to the nucleus greatly preceded its loss from the chloroplast and involved the gain of an intron.

The Sendai virus P gene expresses both an essential protein and an inhibitor of RNA synthesis by shuffling modules via mRNA editing.

Structure, expression and in vitro functional characterization of a novel RNA binding zinc finger protein from Xenopus.

In vitro translation of Plasmodium falciparum aldolase is not initiated at an unusual site.

Interaction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA.

The 3 A crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination.

A single base change in the acceptor stem of tRNA(3Leu) confers resistance upon Escherichia coli to the calmodulin inhibitor, 48/80.

Year: 1991, Volume: 10, Issue: 9

Year: 1991, Volume: 10, Issue: 8

Year: 1991, Volume: 10, Issue: 7

Year: 1991, Volume: 10, Issue: 6

Year: 1991, Volume: 10, Issue: 5

Year: 1991, Volume: 10, Issue: 4

Year: 1991, Volume: 10, Issue: 3

Year: 1991, Volume: 10, Issue: 2

Year: 1991, Volume: 10, Issue: 1

Year: 1990, Volume: 9

Year: 1989, Volume: 8

Year: 1988, Volume: 7

Year: 1987, Volume: 6

Year: 1986, Volume: 5

Year: 1985, Volume: 4

Year: 1984, Volume: 3

Year: 1983, Volume: 2

Year: 1982, Volume: 1

Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum.

Content Provider	PubMed Central
Author	Bonifacino, J. S. Cosson, P. Shah, N. Klausner, R. D.
Abstract	The selective breakdown of newly synthesized proteins retained within the endoplasmic reticulum (ER) is probably mediated by the specific recognition of structural features of protein substrates by components of a degradative system. Within the alpha chain of the multisubunit T-cell antigen receptor (TCR) complex, a transmembrane sequence containing two basic amino acid residues has been shown to act as a determinant for retention and rapid degradation in the ER. We now demonstrate that single basic or acidic amino acid residues can cause targeting for retention and degradation in the ER when placed within the transmembrane domain of an integral membrane protein normally destined for the cell surface. The effect of such potentially charged residues is dependent on their relative position within the transmembrane sequence and on the nature of the amino acid side chains. The phenotypic changes induced by potentially charged transmembrane residues occur without apparent alterations of the global folding or transmembrane topology of the mutant proteins. These observations test the hypothesis that potentially charged residues within transmembrane domains can provide the basis for a motif for ER degradation and explain the selective breakdown of some proteins retained within the ER.
Starting Page	2783
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	10
Volume Number	10
Language	English
Publisher Date	1991-10-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

Central Library (ISO-9001:2015 Certified)
Indian Institute of Technology Kharagpur
Kharagpur, West Bengal, India | PIN - 721302

See location in the Map
03222 282435
Mail: support@ndl.gov.in

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