scholarly journals CD90/Thy-1, a Cancer-Associated Cell Surface Signaling Molecule

2019 ◽  
Vol 7 ◽  
Author(s):  
Chloé Sauzay ◽  
Konstantinos Voutetakis ◽  
Aristotelis Chatziioannou ◽  
Eric Chevet ◽  
Tony Avril
Keyword(s):  
Cell Surface ◽  
Signaling Molecule ◽  
Surface Signaling ◽  
Cell Surface Signaling

scholarly journals Human tumor-derived exosomes (TEX) regulate Treg functions via cell surface signaling rather than uptake mechanisms

2017 ◽  
Vol 6 (8) ◽  
pp. e1261243 ◽  
Author(s):  
Laurent Muller ◽  
Patricia Simms ◽  
Chang-Sook Hong ◽  
Michael I. Nishimura ◽  
Edwin K. Jackson ◽  
...  
Keyword(s):  
Cell Surface ◽  
Human Tumor ◽  
Surface Signaling ◽  
Cell Surface Signaling ◽  
Uptake Mechanisms

Observing Cell Surface Signaling Domains Using Electron Microscopy

2003 ◽  
Vol 2003 (177) ◽  
pp. pl9-pl9 ◽  
Author(s):  
I. A. Prior ◽  
R. G. Parton ◽  
J. F. Hancock
Keyword(s):  
Electron Microscopy ◽  
Cell Surface ◽  
Surface Signaling ◽  
Cell Surface Signaling ◽  
Signaling Domains

scholarly journals Role of Cell Surface Signaling in Proteolysis of an Alternative Sigma Factor in Pseudomonas aeruginosa

2008 ◽  
Vol 190 (14) ◽  
pp. 4865-4869 ◽  
Author(s):  
Matthew R. Spencer ◽  
Paul A. Beare ◽  
Iain L. Lamont
Keyword(s):  
Cell Surface ◽  
Signaling Pathway ◽  
Sigma Factor ◽  
Receptor Protein ◽  
Proteolytic Degradation ◽  
Alternative Sigma Factor ◽  
A Cell ◽  
Surface Signaling ◽  
Cell Surface Signaling ◽  
Antisigma Factor

ABSTRACT Alternative sigma factor proteins enable transcription of specific sets of genes in bacterial cells. Their activities can be controlled by posttranslational mechanisms including inhibition by antisigma proteins and proteolytic degradation. PvdS is an alternative sigma factor that is required for expression of genes involved in synthesis of a siderophore, pyoverdine, by Pseudomonas aeruginosa. In the absence of pyoverdine, the activity of PvdS is inhibited by a membrane-spanning antisigma factor, FpvR. Inhibition is relieved by a cell surface signaling pathway. In this pathway, a combination of pyoverdine and a cell surface receptor protein, FpvA, suppresses the antisigma activity of FpvR, enabling transcription of PvdS-dependent genes. In this research, we investigated proteolytic degradation of PvdS in response to the signaling pathway. Proteolysis of PvdS was observed in strains of P. aeruginosa in which FpvR had anti-sigma factor activity due to the absence of pyoverdine or the FpvA receptor protein or overproduction of FpvR. Suppression of antisigma activity by addition of pyoverdine or through the absence of FpvR prevented detectable proteolysis of PvdS. The amounts of PvdS were less in bacteria in which proteolysis was observed, and reporter gene assays showed that this reduction was not due to decreased expression of PvdS. In wild-type bacteria, there was an average of 730 molecules of PvdS per cell in late exponential growth phase. Our results show that proteolysis and amounts of PvdS are affected by the antisigma factor FpvR and that this activity of FpvR is controlled by the cell surface signaling pathway.

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