Role of membrane phospholipids and glycolipids in the Vero cell surface receptor for rubella virus

1990 ◽  
Vol 179 (2) ◽  
Author(s):  
P. Mastromarino ◽  
L. Cio� ◽  
S. Rieti ◽  
N. Orsi
Keyword(s):  
Cell Surface ◽  
Vero Cell ◽  
Rubella Virus ◽  
Cell Surface Receptor ◽  
Membrane Phospholipids ◽  
Surface Receptor

scholarly journals Unraveling the sugar code: the role of microbial extracellular glycans in plant–microbe interactions

2020 ◽  
Author(s):  
Alan Wanke ◽  
Milena Malisic ◽  
Stephan Wawra ◽  
Alga Zuccaro
Keyword(s):  
Cell Surface ◽  
Hydrolytic Enzymes ◽  
Cell Surface Receptor ◽  
Molecular Signatures ◽  
Receptor Proteins ◽  
Surface Receptor ◽  
Microbe Interactions ◽  
Cell Surface Glycoconjugates ◽  
Cell Surface Glycans

Abstract To defend against microbial invaders but also to establish symbiotic programs, plants need to detect the presence of microbes through the perception of molecular signatures characteristic of a whole class of microbes. Among these molecular signatures, extracellular glycans represent a structurally complex and diverse group of biomolecules that has a pivotal role in the molecular dialog between plants and microbes. Secreted glycans and glycoconjugates such as symbiotic lipochitooligosaccharides or immunosuppressive cyclic β-glucans act as microbial messengers that prepare the ground for host colonization. On the other hand, microbial cell surface glycans are important indicators of microbial presence. They are conserved structures normally exposed and thus accessible for plant hydrolytic enzymes and cell surface receptor proteins. While the immunogenic potential of bacterial cell surface glycoconjugates such as lipopolysaccharides and peptidoglycan has been intensively studied in the past years, perception of cell surface glycans from filamentous microbes such as fungi or oomycetes is still largely unexplored. To date, only few studies have focused on the role of fungal-derived cell surface glycans other than chitin, highlighting a knowledge gap that needs to be addressed. The objective of this review is to give an overview on the biological functions and perception of microbial extracellular glycans, primarily focusing on their recognition and their contribution to plant–microbe interactions.

scholarly journals CYRI-A regulates macropinocytic cup maturation and mediates integrin uptake, limiting invasive migration

2020 ◽  
Author(s):  
Anh Hoang Le ◽  
Tamas Yelland ◽  
Nikki Paul ◽  
Loic Fort ◽  
Savvas Nikolaou ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Ewing Sarcoma ◽  
Negative Regulator ◽  
Cell Surface Receptor ◽  
Actin Dynamics ◽  
Surface Receptor ◽  
Sarcoma Cells ◽  
Wave Complex

The Scar/WAVE complex is the major driver of actin nucleation at the plasma membrane, resulting in lamellipodia and membrane ruffles. While lamellipodia aid migration, membrane ruffles can generate macropinosomes - cup-like structures - important for nutrient uptake and regulation of cell surface receptor levels. How macropinosomes are formed and the role of the actin machinery in their formation and resolution is still not well understood. Mammalian CYRI-B is a recently described negative regulator of the Scar/WAVE complex by RAC1 sequestration, but its other paralogue, CYRI-A has not been characterised. Here we implicate CYRI-A as a key regulator of macropinocytosis maturation and integrin internalisation from the cell surface. We find that CYRI-A is recruited to nascent macropinosomes in a transient but distinct burst, downstream of PIP3-mediated RAC1 activation to regulate actin polymerisation. CYRI-A precedes RAB5A recruitment to engulfed macropinocytic cups and departs as RAB5A is recruited, consistent with a role for CYRI-A as a local suppressor of actin dynamics, enabling the resolution of the macropinocytic cup. The suppression of integrin a5b1 uptake caused by the co-depletion of CYRI-A and B in Ewing sarcoma cells, leads to an enhancement of surface integrin levels and enhanced invasion and anchorage-independent growth in 3D. Thus CYRI-A is a dynamic regulator of integrin uptake via macropinocytosis, functioning together with CYRI-B to regulate integrin homeostasis on the cell surface.

scholarly journals Role of Asparagine-Linked Glycosylation in Cell Surface Expression and Function of the Human Adrenocorticotropin Receptor (Melanocortin 2 Receptor) in 293/FRT Cells

Endocrinology ◽  
2010 ◽  
Vol 151 (2) ◽  
pp. 660-670 ◽  
Author(s):  
Simon Roy ◽  
Benoît Perron ◽  
Nicole Gallo-Payet
Keyword(s):  
Cell Surface ◽  
Fold Increase ◽  
Surface Expression ◽  
Site Directed Mutagenesis ◽  
Cell Surface Receptor ◽  
Cell Surface Expression ◽  
Camp Production ◽  
Glycosylation Sites ◽  
Surface Receptor

Asparagine-linked glycosylation (N-glycosylation) of G protein-coupled receptors may be necessary for functions ranging from agonist binding, folding, maturation, stability, and internalization. Human melanocortin 2 receptor (MC2R) possesses putative N-glycosylation sites in its N-terminal extracellular domain; however, to date, the role of MC2R N-glycosylation has yet to be investigated. The objective of the present study is to examine whether N-glycosylation is essential or not for cell surface expression and cAMP production in native and MC2R accessory protein (MRAPα, -β, or -dCT)-expressing cells using 293/FRT transfected with Myc-MC2R. Western blot analyses performed with or without endoglycosidase H, peptide:N-glycosidase F or tunicamycin treatments and site-directed mutagenesis revealed that MC2R was glycosylated in the N-terminal domain at its two putative N-glycosylation sites (Asn12-Asn13-Thr14 and Asn17-Asn18-Ser19). In the absence of human MRAP coexpression, N-glycosylation of at least one of the two sites was necessary for MC2R cell surface expression. However, when MRAP was present, cell surface expression of MC2R mutants was either rescued entirely with the N17-18Q (QQNN) and N12-13Q (NNQQ) mutants or partially with the unglycosylated N12-13, 17-18Q (QQQQ) mutant. Functional and expression analyses revealed a discrepancy between wild-type (WT) and QQQQ cell surface receptor levels and maximal cAMP production with a 4-fold increase in EC50 values. Taken together, these results indicate that the absence of MC2R N-glycosylation abrogates to a large extent MC2R cell surface expression in the absence of MRAPs, whereas when MC2R is N-glycosylated, it can be expressed at the plasma membrane without MRAP assistance.

The Role of Phosphatidylinositol 4,5 Bisphosphate Breakdown in Cell-Surface Receptor Activation

1984 ◽  
Vol 4 (1-6) ◽  
pp. 489-504 ◽  
Author(s):  
C. J. Kirk ◽  
E. A. Bone ◽  
S. Palmer ◽  
R. H. Michell
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals Lyn controls chemotaxis and motility of CLL cells via phosphorylation of ROR1

2020 ◽  
Author(s):  
Zankruti Dave ◽  
Olga Vondálová Blanářová ◽  
Štěpán Čada ◽  
Pavlína Janovská ◽  
Nikodém Zezula ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Receptor ◽  
Kinase Domain ◽  
Lymphocytic Leukemia ◽  
Cell Surface Receptor ◽  
Surface Dynamics ◽  
Lyn Kinase ◽  
Mantle Cell ◽  
Surface Receptor

AbstractChronic lymphocytic leukemia (CLL) and mantle cell lymphoma (MCL) are malignancies characterized by the dependence on B-cell receptor (BCR) signaling and by the high expression of the cell surface receptor ROR1. Both, BCR and ROR1 are therapeutic targets in these diseases and the understanding of their mutual cross talk is thus of direct therapeutic relevance. In this study we analyzed the role of Lyn, a kinase from the Src family, as a mediator of the BCR-ROR1 crosstalk. We confirm the functional interaction between Lyn and ROR1 and demonstrate that Lyn kinase efficiently phosphorylates ROR1 in its kinase domain and aids the recruitment of an E3 ligase c-CBL. The absence of Lyn in Lyn KO Maver-1 cells produced by CRISPR-Cas9 resulted in the increased ROR1 cell surface levels and deregulated migratory properties. Similar correlations between ROR1 surface dynamics, levels of active Lyn and chemotactic properties were confirmed in primary CLL samples. Our data establish Lyn-mediated phosphorylation of ROR1 as a point of crosstalk between BCR and ROR1 signaling pathways.

scholarly journals Mutational analysis of Cys88 of Toll-like receptor 4 highlights the critical role of MD-2 in cell surface receptor expression

2009 ◽  
Vol 21 (8) ◽  
pp. 925-934 ◽  
Author(s):  
C. Nishitani ◽  
M. Takahashi ◽  
H. Mitsuzawa ◽  
T. Shimizu ◽  
S. Ariki ◽  
...  
Keyword(s):  
Cell Surface ◽  
Mutational Analysis ◽  
Critical Role ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Surface Receptor

Role of Natural Killer (NK) Cell Surface Receptor –NKp46– in Primary Influenza A Infection

2015 ◽  
Vol 135 (2) ◽  
pp. AB164
Author(s):  
Moyar Q. Ge ◽  
Blerina Kokalari ◽  
Anisha Kolupoti ◽  
Kerry S. Campbell ◽  
Angela Haczku
Keyword(s):  
Cell Surface ◽  
Natural Killer ◽  
Influenza A ◽  
Nk Cell ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals Dissecting the Role of PCDH7, an Oncogenic Cell Surface Receptor, in Non–Small Cell Lung Cancer

2017 ◽  
Vol 12 (8) ◽  
pp. S1542 ◽  
Author(s):  
X. Zhou ◽  
B.L. Updegraff ◽  
Y. Guo ◽  
M. Peyton ◽  
L. Girard ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cell Surface ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Cell Surface Receptor ◽  
Small Cell Lung ◽  
Surface Receptor

scholarly journals Angiotensin-converting enzyme 2 and COVID-19 in cardiorenal diseases

2021 ◽  
Vol 135 (1) ◽  
pp. 1-17
Author(s):  
Ravindra K. Sharma ◽  
Jing Li ◽  
Suraj Krishnan ◽  
Elaine M. Richards ◽  
Mohan K. Raizada ◽  
...  
Keyword(s):  
Cell Surface ◽  
Angiotensin Converting Enzyme ◽  
Renin Angiotensin System ◽  
Cell Surface Receptor ◽  
Converting Enzyme ◽  
Angiotensin Converting Enzyme 2 ◽  
Surface Receptor ◽  
A Disintegrin And Metalloproteinase ◽  
Novel Coronavirus

Abstract The rapid spread of the novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has brought into focus the key role of angiotensin-converting enzyme 2 (ACE2), which serves as a cell surface receptor required for the virus to enter cells. SARS-CoV-2 can decrease cell surface ACE2 directly by internalization of ACE2 bound to the virus and indirectly by increased ADAM17 (a disintegrin and metalloproteinase 17)-mediated shedding of ACE2. ACE2 is widely expressed in the heart, lungs, vasculature, kidney and the gastrointestinal (GI) tract, where it counteracts the deleterious effects of angiotensin II (AngII) by catalyzing the conversion of AngII into the vasodilator peptide angiotensin-(1-7) (Ang-(1-7)). The down-regulation of ACE2 by SARS-CoV-2 can be detrimental to the cardiovascular system and kidneys. Further, decreased ACE2 can cause gut dysbiosis, inflammation and potentially worsen the systemic inflammatory response and coagulopathy associated with SARS-CoV-2. This review aims to elucidate the crucial role of ACE2 both as a regulator of the renin–angiotensin system and a receptor for SARS-CoV-2 as well as the implications for Coronavirus disease 19 and its associated cardiovascular and renal complications.

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