scholarly journals Isolation of Arabidopsis extracellular ATP‐binding proteins by affinity proteomics and identification of PHOSPHOLIPASE C‐LIKE 1 as an extracellular protein essential for fumonisin B1 toxicity

2021 ◽  
Author(s):  
Sarah J. Smith ◽  
Heather Goodman ◽  
Johan T.M. Kroon ◽  
Adrian P. Brown ◽  
William J. Simon ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Binding Proteins ◽  
Fumonisin B1 ◽  
Extracellular Atp ◽  
Extracellular Protein ◽  
Atp Binding ◽  
Affinity Proteomics

scholarly journals Phosphatidylinositol-specific phospholipase C activity of chromaffin granule-binding proteins.

1985 ◽  
Vol 260 (12) ◽  
pp. 7171-7173 ◽  
Author(s):  
C E Creutz ◽  
L G Dowling ◽  
E M Kyger ◽  
R C Franson
Keyword(s):  
Phospholipase C ◽  
Binding Proteins ◽  
Chromaffin Granule

scholarly journals Isotope-Coded ATP Probe for Quantitative Affinity Profiling of ATP-Binding Proteins

2013 ◽  
Vol 85 (15) ◽  
pp. 7478-7486 ◽  
Author(s):  
Yongsheng Xiao ◽  
Lei Guo ◽  
Yinsheng Wang
Keyword(s):  
Binding Proteins ◽  
Atp Binding

Inositol-1,4,5-trisphosphate-binding proteins controlling the phototransduction cascade of invertebrate visual cells

2001 ◽  
Vol 204 (3) ◽  
pp. 487-493
Author(s):  
A. Kishigami ◽  
T. Ogasawara ◽  
Y. Watanabe ◽  
M. Hirata ◽  
T. Maeda ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Binding Proteins ◽  
Affinity Column ◽  
Receptor Kinase ◽  
Nucleotide Exchange ◽  
Visual Cells ◽  
Signal Cascade ◽  
Phosphatidylinositol Turnover ◽  
Inositol 1,4,5 Trisphosphate ◽  
Phototransduction Cascade

The main phototransduction cascade in invertebrate visual cells involves the turnover of phosphatidylinositol, an important biochemical mechanism common to many signal-transduction systems. Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol. Subsequently, inositol-1,4,5-trisphosphate-binding proteins continue the signal cascade. Here, we report on the first inositol-1,4,5-trisphosphate-binding proteins demonstrated in an invertebrate visual system with our investigation of the photosensitive rhabdoms of squid. We screened the ability of proteins to interact with inositol-1,4,5-trisphosphate by affinity column chromatography with an inositol-1,4,5-trisphosphate analogue. We detected an inositol-1,4,5-trisphosphate-binding affinity in phospholipase C, receptor kinase and five other proteins in the cytosolic fraction and, surprisingly, rhodopsin in the membrane fraction. A binding assay with (3)H-labelled inositol-1,4,5-trisphosphate demonstrated the inositol-1,4,5-trisphosphate affinity of each of the purified proteins. Since rhodopsin, receptor kinase and phospholipase C are involved upstream of phosphatidylinositol turnover in the signal cascade, our result suggests that phosphatidylinositol turnover is important in feedback pathways in the signalling system.

scholarly journals Affinity labeling of annexin VI with a triazine dye, Cibacron blue 3GA. Probable interaction of the dye with C-terminal nucleotide-binding site within the annexin molecule.

1999 ◽  
Vol 46 (2) ◽  
pp. 419-429 ◽  
Author(s):  
M Danieluk ◽  
R Buś ◽  
S Pikuła ◽  
J Bandorowicz-Pikuła
Keyword(s):  
Binding Site ◽  
Binding Proteins ◽  
Direct Sequencing ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Dependent Manner ◽  
Cibacron Blue ◽  
Annexin Vi ◽  
Cibacron Blue 3Ga ◽  
Triazine Dye

Annexin VI (AnxVI) from porcine liver, a member of the annexin family of Ca(2+)- and membrane-binding proteins, has been shown to bind ATP in vitro with a K(d) in the low micromolar concentration range. However, this protein does not contain within its primary structure any ATP-binding consensus motifs found in other nucleotide-binding proteins. In addition, binding of ATP to AnxVI resulted in modulation of AnxVI function, which was accompanied by changes in AnxVI affinity to Ca2+ in the presence of ATP. Using limited proteolytic digestion, purification of protein fragments by affinity chromatography on ATP-agarose, and direct sequencing, the ATP-binding site of AnxVI was located in a C-terminal half of the AnxVI molecule. To further study AnxVI-nucleotide interaction we have employed a functional nucleotide analog, Cibacron blue 3GA (CB3GA), a triazine dye which is commonly used to purify multiple ATP-binding proteins and has been described to modulate their activities. We have observed that AnxVI binds to CB3GA immobilized on agarose in a Ca(2+)-dependent manner. Binding is reversed by EGTA and by ATP and, to a lower extent, by other adenine nucleotides. CB3GA binds to AnxVI also in solution, evoking reversible aggregation of protein molecules, which resembles self-association of AnxVI molecules either in solution or on a membrane surface. Our observations support earlier findings that AnxVI is an ATP-binding protein.

scholarly journals The ABCF gene family facilitates disaggregation during animal development

2020 ◽  
Vol 31 (13) ◽  
pp. 1324-1345
Author(s):  
Sydney Skuodas ◽  
Amy Clemons ◽  
Michael Hayes ◽  
Ashley Goll ◽  
Betul Zora ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Gene Family ◽  
Early Development ◽  
Binding Proteins ◽  
Atp Binding ◽  
Animal Development ◽  
Developmental Program ◽  
Animal Genomes

Skuodas and Clemons et al. show that protein aggregation is pervasive during early development and that the ABCF family of soluble ATP-binding proteins, which are encoded by animal genomes and expressed embryonically, regulate disaggregation and are instrumental for a normal developmental program.

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