scholarly journals Substance P downregulates expression of the high affinity IgE receptor (FcεRI) by human mast cells

2010 ◽  
Vol 220 (1-2) ◽  
pp. 17-24 ◽  
Author(s):  
Christine McCary ◽  
Brian P. Tancowny ◽  
Adriana Catalli ◽  
Leslie C. Grammer ◽  
Kathleen E. Harris ◽  
...  
2008 ◽  
Vol 336 (2) ◽  
pp. 229-234 ◽  
Author(s):  
Akira Matsuda ◽  
Yoshimichi Okayama ◽  
Nobuyuki Ebihara ◽  
Norihiko Yokoi ◽  
Peisong Gao ◽  
...  

2012 ◽  
Vol 157 (3) ◽  
pp. 246-250 ◽  
Author(s):  
Hans Jürgen Hoffmann ◽  
Pernille Munk Frandsen ◽  
Lars Harder Christensen ◽  
Peter Oluf Schiøtz ◽  
Ronald Dahl

1996 ◽  
Vol 8 (9) ◽  
pp. 1367-1373 ◽  
Author(s):  
Hano Toru, Chisel Ra ◽  
Shigeaki Nonoyama ◽  
Katsuhiro Suzuki ◽  
Jun-ichi Yata ◽  
Tatsutoshi Nakahata ◽  
...  

2011 ◽  
Vol 127 (2) ◽  
pp. AB133-AB133 ◽  
Author(s):  
H. Hoffmann ◽  
P. Munk Frandsen ◽  
L. Harder Christensen ◽  
R. Dahl ◽  
P. Schiøtz

2017 ◽  
Vol 37 (7) ◽  
Author(s):  
Xiaocui Zhang ◽  
Geneviève Lavoie ◽  
Antoine Méant ◽  
Léo Aubert ◽  
Marie Cargnello ◽  
...  

ABSTRACT The scaffolding adapter protein Gab2 (Grb2-associated binder) promotes cell proliferation, survival, and motility by engaging several signaling pathways downstream of growth factor and cytokine receptors. In particular, Gab2 plays essential roles in mast cells, as it is required for phosphoinositide 3-kinase (PI3K) activation in response to Kit and the high-affinity IgE receptor. While the positive role of Gab2 in PI3K signaling is well documented, very little is known about the mechanisms that attenuate its function. Here we show that Gab2 becomes phosphorylated on multiple proline-directed sites upon stimulation of the Ras/extracellular signal-regulated kinase (ERK) signaling pathway. We demonstrate that ERK1 and ERK2 interact with Gab2 via a novel docking motif, which is required for subsequent Gab2 phosphorylation in response to ERK1/2 activation. We identified four ERK1/2-dependent phosphorylation sites in Gab2 that prevent the recruitment of the p85 regulatory subunit of PI3K. Using bone marrow-derived mast cells to study Gab2-dependent signaling, we found that the inhibition of ERK1/2 activity promotes Akt signaling in response to Kit and the high-affinity IgE receptor. Together, our results indicate that ERK1/2 participates in a negative-feedback loop that attenuates PI3K/Akt signaling in response to various agonists.


2009 ◽  
Vol 184 (1) ◽  
pp. 84-93 ◽  
Author(s):  
Michael Poderycki ◽  
Yoshiaki Tomimori ◽  
Tomoaki Ando ◽  
Wenbin Xiao ◽  
Mari Maeda-Yamamoto ◽  
...  

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e109800 ◽  
Author(s):  
Asma Kassas ◽  
Ivan C. Moura ◽  
Yumi Yamashita ◽  
Jorg Scheffel ◽  
Claudine Guérin-Marchand ◽  
...  

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