The Apoptosis-Inducing Protein Kinase DRAK2 Is Inhibited in a Calcium-Dependent Manner by the Calcium-Binding Protein CHP

2003 ◽  
Vol 134 (2) ◽  
pp. 245-250 ◽  
Author(s):  
H. Kuwahara
Keyword(s):  
Protein Kinase ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Dependent Manner ◽  
Calcium Dependent

scholarly journals A novel protein kinase from Brassica juncea stimulated by a protozoan calcium binding protein

2000 ◽  
Vol 267 (11) ◽  
pp. 3181-3189 ◽  
Author(s):  
Renu Deswal ◽  
Girdhar K Pandey ◽  
Meena Rani Chandok ◽  
Nagendra Yadav ◽  
Alok Bhattacharya ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Brassica Juncea ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Novel Protein

scholarly journals Calcium-binding protein S100A6 interaction with VEGF receptors integrates signaling and trafficking pathways

2021 ◽  
Author(s):  
Sreenivasan Ponnambalam ◽  
Leyuan Bao ◽  
Gareth W Fearnley ◽  
Chi-Chuan Lin ◽  
Adam F Odell ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Calcium Binding ◽  
Mapk Pathway ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Mitogen Activated Protein Kinase ◽  
Tyrosine Kinase Domain ◽  
Dependent Manner ◽  
Endothelial Cell Function

The mammalian endothelium which lines all blood vessels responds to soluble factors which control vascular development and sprouting. Endothelial cells bind to vascular endothelial growth factor A via two different receptor tyrosine kinases (VEGFR1, VEGFR2) which regulate such cellular responses. The integration of VEGFR signal transduction and membrane trafficking is not well understood. Here, we used a yeast-based membrane protein screen to identify VEGFR-interacting factor(s) which modulate endothelial cell function. By screening a human endothelial cDNA library, we identified a calcium-binding protein, S100A6, which can interact with either VEGFR. We found that S100A6 binds in a calcium-dependent manner to either VEGFR1 or VEGFR2. S100A6 binding was mapped to the VEGFR2 tyrosine kinase domain. Depletion of S100A6 impacts on VEGF-A-regulated signaling through the canonical mitogen-activated protein kinase (MAPK) pathway. Furthermore, S100A6 depletion caused contrasting effects on biosynthetic VEGFR delivery to the plasma membrane. Co-distribution of S100A6 and VEGFRs on tubular profiles suggest the presence of transport carriers that facilitate VEGFR trafficking. We propose a mechanism whereby S100A6 acts as a calcium regulated switch which facilitates biosynthetic VEGFR trafficking from the TGN-to-plasma membrane. VEGFR-S100A6 interactions thus enable integration of signaling and trafficking pathways in controlling the endothelial response to VEGF-A.

scholarly journals Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin

1994 ◽  
Vol 124 (5) ◽  
pp. 757-768 ◽  
Author(s):  
K Takenaga ◽  
Y Nakamura ◽  
S Sakiyama ◽  
Y Hasegawa ◽  
K Sato ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
S100 Protein ◽  
Calcium Binding Protein ◽  
Immunofluorescent Staining ◽  
Dependent Manner ◽  
3T3 Cells ◽  
Cell Extracts ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

The cDNA coding for mouse fibroblast tropomyosin isoform 2 (TM2) was placed into a bacterial expression vector to produce a fusion protein containing glutathione-S-transferase (GST) and TM2 (GST/TM2). Glutathione-Sepharose beads bearing GST/TM2 were incubated with [35S]methionine-labeled NIH 3T3 cell extracts and the materials bound to the fusion proteins were analyzed to identify proteins that interact with TM2. A protein of 10 kD was found to bind to GST/TM2, but not to GST. The binding of the 10-kD protein to GST/TM2 was dependent on the presence of Ca2+ and inhibited by molar excess of free TM2 in a competition assay. The 10-kD protein-binding site was mapped to the region spanning residues 39-107 on TM2 by using several COOH-terminal and NH2-terminal truncation mutants of TM2. The 10-kD protein was isolated from an extract of NIH 3T3 cells transformed by v-Ha-ras by affinity chromatography on a GST/TM2 truncation mutant followed by SDS-PAGE and electroelution. Partial amino acid sequence analysis of the purified 10-kD protein, two-dimensional polyacrylamide gel analysis and a binding experiment revealed that the 10-kD protein was identical to a calcium-binding protein derived from mRNA named pEL98 or 18A2 that is homologous to S100 protein. Immunoblot analysis of the distribution of the 10-kD protein in Triton-soluble and -insoluble fractions of NIH 3T3 cells revealed that some of the 10-kD protein was associated with the Triton-insoluble cytoskeletal residue in a Ca(2+)-dependent manner. Furthermore, immunofluorescent staining of NIH 3T3 cells showed that some of the 10-kD protein colocalized with nonmuscle TMs in microfilament bundles. These results suggest that some of the pEL98 protein interacts with microfilament-associated nonmuscle TMs in NIH 3T3 cells.

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