scholarly journals Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding protein in T and B lymphocytes

FEBS Open Bio ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 255-259 ◽  
Author(s):  
Hiroshi Matsuzaki ◽  
Takahiro Fujimoto ◽  
Takeharu Ota ◽  
Masahiro Ogawa ◽  
Toshiyuki Tsunoda ◽  
...  
Keyword(s):  
B Lymphocytes ◽  
Receptor Binding ◽  
Binding Protein ◽  
T And B Lymphocytes ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Receptor Binding Protein

scholarly journals Protein phosphatase-1 is a novel regulator of the interaction between IRBIT and the inositol 1,4,5-trisphosphate receptor

2007 ◽  
Vol 407 (2) ◽  
pp. 303-311 ◽  
Author(s):  
Benoit Devogelaere ◽  
Monique Beullens ◽  
Eva Sammels ◽  
Rita Derua ◽  
Etienne Waelkens ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Phosphorylation Sites ◽  
Docking Site ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Receptor Binding Protein

IRBIT is an IP3R [IP3 (inositol 1,4,5-trisphosphate) receptor]-binding protein that competes with IP3 for binding to the IP3R. Phosphorylation of IRBIT is essential for the interaction with the IP3R. The unique N-terminal region of IRBIT, residues 1–104 for mouse IRBIT, contains a PEST (Pro-Glu-Ser-Thr) domain with many putative phosphorylation sites. In the present study, we have identified a well-conserved PP1 (protein phosphatase-1)-binding site preceeding this PEST domain which enabled the binding of PP1 to IRBIT both in vitro and in vivo. IRBIT emerged as a mediator of its own dephosphorylation by associated PP1 and, hence, as a novel substrate specifier for PP1. Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R by IRBIT. Finally, we have shown that mutational inactivation of the docking site for PP1 on IRBIT increased the affinity of IRBIT for the IP3R. This pinpoints PP1 as a key player in the regulation of IP3R-controlled Ca2+ signals.

scholarly journals F1Aα, a Death Receptor-binding Protein Homologous to theCaenorhabditis elegansSex-determining Protein, FEM-1, Is a Caspase Substrate That Mediates Apoptosis

1999 ◽  
Vol 274 (45) ◽  
pp. 32461-32468 ◽  
Author(s):  
Shing-Leng Chan ◽  
Kuan-Onn Tan ◽  
Li Zhang ◽  
Karen S. Y. Yee ◽  
Francesca Ronca ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Protein ◽  
Death Receptor ◽  
Caspase Substrate ◽  
Receptor Binding Protein

Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe

The Analyst ◽  
2011 ◽  
Vol 136 (22) ◽  
pp. 4780 ◽  
Author(s):  
Amit Singh ◽  
Denis Arutyunov ◽  
Mark T. McDermott ◽  
Christine M. Szymanski ◽  
Stephane Evoy
Keyword(s):  
Campylobacter Jejuni ◽  
Receptor Binding ◽  
Binding Protein ◽  
Specific Detection ◽  
Receptor Binding Protein
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