scholarly journals Solubilization and separation of inositol 1,3,4,5-tetrakisphosphate- and inositol 1,4,5-trisphosphate-binding proteins and metabolizing enzymes in rat brain

1990 ◽  
Vol 267 (2) ◽  
pp. 441-445 ◽  
Author(s):  
A B Theibert ◽  
S Supattapone ◽  
C D Ferris ◽  
S K Danoff ◽  
R K Evans ◽  
...  
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Molecular Species ◽  
Binding Proteins ◽  
Inositol Phosphate ◽  
Second Messenger ◽  
Phosphate Binding ◽  
Metabolizing Enzymes ◽  
High Affinity ◽  
Inositol 1,4,5 Trisphosphate

The two inositol phosphate-binding proteins, the Ins(1,4,5)P3 (InsP3) and Ins(1,3,4,5)P4 (InsP4) receptors, and the two particulate InsP3-metabolizing enzymes, InsP3 5-phosphatase and InsP3 3-kinase, were solubilized with detergent from rat cerebellar membranes. These four activities are shown to be distinct molecular species by separation using a variety of protein chromatographic steps. The pharmacology of the partially purified InsP4-binding site indicates that the binding has a high affinity and selectivity for InsP4 over InsP3. These results suggest the existence of a distinct specific InsP4-binding protein which may represent the receptor for this putative second messenger.

scholarly journals Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site

Structure ◽  
2015 ◽  
Vol 23 (2) ◽  
pp. 352-363 ◽  
Author(s):  
Katarina Moravcevic ◽  
Diego Alvarado ◽  
Karl R. Schmitz ◽  
Jon A. Kenniston ◽  
Jeannine M. Mendrola ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Site ◽  
Inositol Phosphate ◽  
Phosphate Binding ◽  
Bar Domain ◽  
Domain Structures

Characterization and mapping of the 12kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor

2001 ◽  
Vol 354 (2) ◽  
pp. 413-422 ◽  
Author(s):  
Geert BULTYNCK ◽  
Patrick DE SMET ◽  
Daniela ROSSI ◽  
Geert CALLEWAERT ◽  
Ludwig MISSIAEN ◽  
...  
Keyword(s):  
Binding Site ◽  
Ryanodine Receptor ◽  
Binding Protein ◽  
Limited Proteolysis ◽  
Ip3 Receptor ◽  
Fk506 Binding Protein ◽  
High Affinity ◽  
Receptor Isoforms ◽  
Inositol 1,4,5 Trisphosphate ◽  
Affinity Interaction

We investigated the interaction of the 12kDa FK506-binding protein (FKBP12) with two ryanodine-receptor isoforms (RyR1 and RyR3) and with two myo-inositol 1,4,5-trisphosphate (IP3) receptor isoforms (IP3R1 and IP3R3). Using glutathione S-transferase (GST)-FKBP12 affinity chromatography, we could efficiently extract RyR1 (42±7% of the solubilized RyR1) from terminal cisternae of skeletal muscle as well as RyR3 (32±4% of the solubilized RyR3) from RyR3-overexpressing HEK-293 cells. These interactions were completely abolished by FK506 (20µM) but were largely unaffected by RyR-channel modulators. In contrast, neither IP3R1 nor IP3R3 from various sources, including rabbit cerebellum, A7r5 smooth-muscle cells and IP3R-overexpressing Sf9 insect cells from Spodoptera frugiperda, were retained on the GST-FKBP12 matrix. Moreover, immunoprecipitation experiments indicated a high-affinity interaction of FKBP12 with RyR1 but not with IP3R1. In order to determine the FKBP12-binding site, we fragmented both RyR1 and IP3R1 by limited proteolysis. We obtained a 45kDa fragment of RyR1 that bound to the GST-FKBP12 matrix, indicating that it retained all requirements for FKBP12 binding. This fragment was identified by its interaction with antibody m34C and must therefore contain its epitope (amino acids 2756–2803). However, no fragment of IP3R1 was retained on the column. These molecular data are in agreement with the lack of correlation between FKBP12 and IP3R1 expression in various cell types. The observation that FKBP12 did not affect IP3-induced Ca2+ release but reduced caffeine-induced Ca2+ release also indicated that mature IP3R1 and IP3R3, in contrast to RyR1 and RyR3, did not display a specific, high-affinity interaction with FKBP12.

scholarly journals Subcellular Localization of a High Affinity Binding Site ford-myo-Inositol 1,4,5-Trisphosphate fromChenopodium rubrum

2000 ◽  
Vol 124 (1) ◽  
pp. 475-483 ◽  
Author(s):  
Jan Martinec ◽  
Tomáš Feltl ◽  
Chris H. Scanlon ◽  
Peter J. Lumsden ◽  
Ivana Macháčková
Keyword(s):  
Subcellular Localization ◽  
Binding Site ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
Inositol 1,4,5 Trisphosphate ◽  
High Affinity Binding Site

High affinity binding site for γ-hydroxybutyric acid in rat brain

Life Sciences ◽  
1982 ◽  
Vol 30 (11) ◽  
pp. 953-961 ◽  
Author(s):  
J. Benavides ◽  
J.F. Rumigny ◽  
J.J. Bourguignon ◽  
C. Cash ◽  
C.G. Wermuth ◽  
...  
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Affinity Binding ◽  
Hydroxybutyric Acid ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

D-myo-Inositol 1,4,5-Trisphosphate-Binding Proteins in Rat Brain Membranes1

1994 ◽  
Vol 115 (5) ◽  
pp. 973-980 ◽  
Author(s):  
Masako Yoshida ◽  
Takashi Kanematsu ◽  
Yutaka Watanabe ◽  
Toshitaka Koga ◽  
Shoichiro Ozaki ◽  
...  
Keyword(s):  
Rat Brain ◽  
Binding Proteins ◽  
Inositol 1,4,5 Trisphosphate

High affinity histamine binding site is the H3 receptor: Characterization and autoradiographic localization in rat brain

Synapse ◽  
1991 ◽  
Vol 8 (2) ◽  
pp. 144-151 ◽  
Author(s):  
Paul Cumming ◽  
Christopher Shaw ◽  
Steven R. Vincent
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
High Affinity ◽  
H3 Receptor ◽  
Histamine Binding

scholarly journals Mycobacterium tuberculosis with Disruption in Genes Encoding the Phosphate Binding Proteins PstS1 and PstS2 Is Deficient in Phosphate Uptake and Demonstrates Reduced In Vivo Virulence

2005 ◽  
Vol 73 (3) ◽  
pp. 1898-1902 ◽  
Author(s):  
Priska Peirs ◽  
Philippe Lefèvre ◽  
Samira Boarbi ◽  
Xiao-Ming Wang ◽  
Olivier Denis ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Life Span ◽  
Binding Proteins ◽  
Phosphate Uptake ◽  
Infection Model ◽  
Phosphate Binding ◽  
High Affinity ◽  
Mouse Infection Model ◽  
Genes Encoding

ABSTRACT By measuring phosphate uptake by Mycobacterium tuberculosis strains with the pstS1 and pstS2 genes genetically inactivated, we showed that these pstS genes encode high-affinity phosphate binding proteins. In a mouse infection model, both mutants were attenuated in virulence, suggesting that M. tuberculosis encounters limiting phosphate concentrations during its intracellular life span.

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