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.

Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17

2003 ◽  
Vol 302 (2) ◽  
pp. 186-192 ◽  
Author(s):  
Thierry Dubois ◽  
Steven Howell ◽  
Eva Zemlickova ◽  
Michele Learmonth ◽  
Andy Cronshaw ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Phosphorylation Sites

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

The microtubule- and PP1-binding activities of Drosophila melanogaster Spc105 control the kinetics of SAC satisfaction.

2021 ◽  
Author(s):  
Margaux R. Audett ◽  
Erin L. Johnson ◽  
Jessica M. McGory ◽  
Dylan M. Barcelos ◽  
Evelin Oroszne Szalai ◽  
...  
Keyword(s):  
Protein Binding ◽  
Protein Phosphatase ◽  
Spindle Assembly Checkpoint ◽  
Protein Phosphatase 1 ◽  
Intrinsically Disordered ◽  
Regulatory Circuit ◽  
Cell Assays ◽  
Kinetics Of

KNL1 is a large intrinsically disordered kinetochore (KT) protein that recruits spindle assembly checkpoint (SAC) components to mediate SAC signaling. The N-terminal region (NTR) of KNL1 possesses two activities that have been implicated in SAC silencing: microtubule (MT) binding and protein phosphatase 1 (PP1) recruitment. The NTR of D. melanogaster KNL1 (Spc105) has never been shown to bind MTs nor to recruit PP1. Furthermore, the phospho-regulatory mechanisms known to control SAC protein binding to KNL1 orthologues is absent in D. melanogaster. Here, these apparent discrepancies are resolved using in vitro and cell based-assays. A phospho-regulatory circuit, which utilizes Aurora B kinase (ABK), promotes SAC protein binding to the central disordered region of Spc105 while the NTR binds directly to MTs in vitro and recruits PP1-87B to KTs in vivo. Live-cell assays employing an optogenetic oligomerization tag, and deletion/chimera mutants are used to define the interplay of MT- and PP1-binding by Spc105 and the relative contributions of both activities to the kinetics of SAC satisfaction. [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text] [Media: see text]

Nuclear receptor-binding protein 1: a novel tumour suppressor and pseudokinase

2013 ◽  
Vol 41 (4) ◽  
pp. 1055-1060 ◽  
Author(s):  
Jason S. Kerr ◽  
Catherine H. Wilson
Keyword(s):  
Nuclear Receptor ◽  
Receptor Binding ◽  
Kinase Activity ◽  
Binding Protein ◽  
Kinase Domain ◽  
Present Review ◽  
Critical Components ◽  
Receptor Binding Protein

Pseudokinases are a class of kinases which are structurally designated as lacking kinase activity. Despite the lack of kinase domain sequence conservation, there is increasing evidence that a number of pseudokinases retain kinase activity and/or have critical cellular functions, casting aside previous notions that pseudokinases simply exist as redundant kinases. Moreover, a number of recent studies have implicated pseudokinases as critical components in cancer formation and progression. The present review discusses the interactions and potential functions that nuclear receptor-binding protein 1, a pseudokinase recently described to have a tumour-suppressive role in cancer, may play in cellular homoeostasis and protein regulation. The recent findings highlighted in the present review emphasize the requirement to fully determine the function of pseudokinases in vitro and in vivo, the understanding of which may ultimately uncover new directions for drug discovery.

In Vivo and in Vitro Binding of Microcystin to Protein Phosphatase 1 and 2A

1995 ◽  
Vol 216 (1) ◽  
pp. 162-169 ◽  
Author(s):  
M. Runnegar ◽  
N. Berndt ◽  
S.M. Kong ◽  
E.Y.C. Lee ◽  
L.F. Zhang
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
In Vitro Binding ◽  
Vitro Binding

Protein Phosphatase 1 binds strongly to the retinoblastoma protein but not to p107 or p130 in vitro and in vivo

2002 ◽  
Vol 24 (5) ◽  
pp. 392-396 ◽  
Author(s):  
Joshua L. Dunaief ◽  
Ayala King ◽  
Noriko Esumi ◽  
Matthew Eagen ◽  
Tzvete Dentchev ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Retinoblastoma Protein ◽  
Protein Phosphatase 1
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