scholarly journals Microbial Disease Spectrum Linked to a Novel IL-12Rβ1 N-Terminal Signal Peptide Stop-Gain Homozygous Mutation with Paradoxical Receptor Cell-Surface Expression

2017 ◽  
Vol 8 ◽  
Author(s):  
Thais Louvain de Souza ◽  
Regina C. de Souza Campos Fernandes ◽  
Juliana Azevedo da Silva ◽  
Vladimir Gomes Alves Júnior ◽  
Adelia Gomes Coelho ◽  
...  
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Receptor Cell ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Homozygous Mutation ◽  
Disease Spectrum ◽  
Microbial Disease

scholarly journals Regulation of GIP and GLP1 Receptor Cell Surface Expression by N-Glycosylation and Receptor Heteromerization

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e32675 ◽  
Author(s):  
Gina M. Whitaker ◽  
Francis C. Lynn ◽  
Christopher H. S. McIntosh ◽  
Eric A. Accili
Keyword(s):  
Cell Surface ◽  
Receptor Cell ◽  
Surface Expression ◽  
Cell Surface Expression

scholarly journals Individual cells traffic the Vasopressin 2 Receptor to their cell surface with different success

2021 ◽  
Author(s):  
Eline J Koers ◽  
Bradley A Morgan ◽  
Iain B Styles ◽  
Dmitry J Veprintsev
Keyword(s):  
Cell Surface ◽  
Receptor Cell ◽  
Surface Expression ◽  
G Protein Coupled Receptors ◽  
Cell Surface Expression ◽  
Subcellular Localisation ◽  
Equal Distribution ◽  
Mutant Receptors ◽  
G Protein Coupled ◽  
Correct Expression

G protein coupled receptors (GPCRs) translate the actions of hormones and neurotransmitters into intracellular signalling events. Mutations in GPCRs can prevent their correct expression and trafficking to the cell surface and cause disease. Single cell subcellular localisation measurements reveal that while some cells appear to traffic the majority of the vasopressin 2 receptor (V2R) molecules to the cell surface, others retain a greater number of receptors in the ER or have approximately equal distribution. Mutations in the V2R affect the proportion of cells able to send this GPCR to their cell surface but surprisingly they do not prevent all cells from correctly trafficking the mutant receptors. These findings reveal the potential for rescue of mutant receptor cell surface expression by pharmacological manipulation of the GPCR folding and trafficking machinery.

scholarly journals The PAR2 signal peptide prevents premature receptor cleavage and activation

2019 ◽  
Author(s):  
Belinda Liu ◽  
Grace Lee ◽  
Jiejun Wu ◽  
Janise Deming ◽  
Chester Kuei ◽  
...  
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Synthetic Peptide ◽  
Surface Expression ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Cell Surface Expression ◽  
Peptide Ligand ◽  
Protease Activated Receptors ◽  
N Terminus

AbstractUnlike closely related GPCRs, protease-activated receptors (PAR1, PAR2, PAR3, and PAR4) have a predicted signal peptide at their N-terminus, which is encoded by a separate exon, suggesting that the signal peptides of PARs may serve an important and unique function, specific for PARs. In this report, we show that the PAR2 signal peptide, when fused to the N-terminus of IgG-Fc, effectively induced IgG-Fc secretion into culture medium, thus behaving like a classical signal peptide. The presence of PAR2 signal peptide has a strong effect on PAR2 cell surface expression, as deletion of the signal peptide (PAR2ΔSP) led to dramatic reduction of the cell surface expression and decreased responses to trypsin or the synthetic peptide ligand (SLIGKV). However, further deletion of the tethered ligand region (SLIGKV) at the N-terminus rescued the cell surface receptor expression and the response to the synthetic peptide ligand, suggesting that the signal peptide of PAR2 may be involved in preventing PAR2 from intracellular protease activation before reaching the cell surface. Supporting this hypothesis, an Arg36Ala mutation on PAR2ΔSP, which disabled the trypsin activation site, increased the receptor cell surface expression and the response to ligand stimulation. Similar effects were observed when PAR2ΔSP expressing cells were treated with protease inhibitors. Our findings indicated that these is a role of the PAR2 signal peptide in preventing the premature activation of PAR2 from intracellular protease cleavage before reaching the cells surface. The same mechanism may also apply to PAR1, PAR3, and PAR4.

CLIC4 interacts with histamine H3 receptor and enhances the receptor cell surface expression

2008 ◽  
Vol 369 (2) ◽  
pp. 603-608 ◽  
Author(s):  
Kay Maeda ◽  
Mitsuya Haraguchi ◽  
Atsuo Kuramasu ◽  
Takeya Sato ◽  
Kyohei Ariake ◽  
...  
Keyword(s):  
Cell Surface ◽  
Receptor Cell ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Histamine H3 Receptor ◽  
H3 Receptor ◽  
Histamine H3

scholarly journals P2X7 Receptor Cell Surface Expression and Cytolytic Pore Formation Are Regulated by a Distal C-terminal Region

2002 ◽  
Vol 278 (10) ◽  
pp. 8853-8860 ◽  
Author(s):  
Megan L. Smart ◽  
Ben Gu ◽  
Rekha G. Panchal ◽  
James Wiley ◽  
Brett Cromer ◽  
...  
Keyword(s):  
Cell Surface ◽  
P2x7 Receptor ◽  
Pore Formation ◽  
Receptor Cell ◽  
Surface Expression ◽  
Terminal Region ◽  
Cell Surface Expression

Two Different β3 Cysteine Substitutions Alter αIIbβ3 Maturation and Result in Glanzmann Thrombasthenia

2002 ◽  
Vol 88 (07) ◽  
pp. 104-110 ◽  
Author(s):  
S. Milet-Marsal ◽  
C. Breillat ◽  
O. Peyruchaud ◽  
P. Nurden ◽  
R. Combrié ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Transient Expression ◽  
Double Mutant ◽  
Direct Sequencing ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Homozygous Mutation ◽  
Glanzmann Thrombasthenia ◽  
Exon 10

SummaryWe report the defects responsible for Glanzmann thrombasthenia in two patients showing traces of abnormally migrating platelet β3 in immunoblotting. Using PCR-SSCP and direct sequencing, we identified a novel homozygous mutation in exon 10 of the β3 gene of patient 1 which gave a C457 to Y amino acid substitution. A C542 to R substitution in β3 of patient 2 was previously reported by us. These cysteines are present in EGF-domains 1 and 3 respectively of β3. We therefore constructed mutants carrying substitutions on cysteine residues in each of the first three EGF domains of β3, C457, C495 and C542 respectively. Transient expression of these mutants in COS-7 cells, including the C542 and C547 double mutant, proved that disulfide disruption directly affects cell surface expression of the integrin. We then showed by metabolic (35S) labeling and Endo-H glycosidase treatment that these substitutions strongly affected complex maturation within the cell.

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