scholarly journals Protein-protein Interaction Analysis of Contributing Molecules in Dura mater Healing Process

2020 ◽  
Vol 13 (3) ◽  
pp. 73-82
Author(s):  
Hendrikus Masang Ban Bolly ◽  
Yulius Hermanto ◽  
Ahmad Faried ◽  
Muhammad Zafrullah Arifin ◽  
Trajanus Laurens Yembise ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Dura Mater ◽  
Protein Interaction ◽  
Confidence Level ◽  
Interaction Analysis ◽  
Healing Process ◽  
Brain Anatomy ◽  
Mesenchymal Transition ◽  
Protein Protein Interaction

Background: Dura mater is a special tissue that fulfills a critical function in brain anatomy and physiology. This tissue contains numerous cells, stem cells, and growth factors. This research investigates the protein interaction contributing to dura mater healing process. Methods: We use the available analysis software to perform the protein-protein interaction (PPI) analysis (http://gpsprot.org/index.php). GPS Protein is an interactive platform for visualizing human protein interaction by integrating HIPPIE and CORUM databases. We excluded HIV-1 proteomic and RNAi databases, instead focused on human PPI (Confidence level 0.75). Two proteins were inputted as query to identify the potential protein network in Dura mater healing according to previous studies, i.e. fibroblast growth factor-2 (FGF2) and transforming growth factor beta-1 (TGFβ1). Results: PPI results shows a high level (confidence level > 0.75) of protein-protein interaction of TGFβ1 to 197 other proteins (Confidence level ranges: 0.49 - 0.87), and PPI of FGF2 to 26 other proteins (Confidence level ranges: 0.0-0.97). TGFβ1 interactions showed the important interactions to some remodeling proteins. TGFβ1 encoded regulates cell proliferation, differentiation, growth, expression modulation and the activation of other growth factors. It also induces epithelial-to-mesenchymal transition (EMT) and cell migration. Conclusion: This bioinformatics approach is the more efficient and cheaper method for analyzing the molecular aspect of protein that has a special contribution in Dura mater healing process. These results could beneficial in focusing further researches for more complex laboratory examinations.

scholarly journals Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin

2014 ◽  
Vol 25 (22) ◽  
pp. 3654-3671 ◽  
Author(s):  
Changsheng Lin ◽  
Jason Ear ◽  
Krishna Midde ◽  
Inmaculada Lopez-Sanchez ◽  
Nicolas Aznar ◽  
...  
Keyword(s):  
Growth Factor ◽  
G Proteins ◽  
Protein Interaction ◽  
Cross Talk ◽  
Tyrosine Kinases ◽  
Molecular Mechanisms ◽  
Growth Factor Receptors ◽  
Structural Basis ◽  
Nucleotide Exchange ◽  
Protein Protein Interaction

A long-standing issue in the field of signal transduction is to understand the cross-talk between receptor tyrosine kinases (RTKs) and heterotrimeric G proteins, two major and distinct signaling hubs that control eukaryotic cell behavior. Although stimulation of many RTKs leads to activation of trimeric G proteins, the molecular mechanisms behind this phenomenon remain elusive. We discovered a unifying mechanism that allows GIV/Girdin, a bona fide metastasis-related protein and a guanine-nucleotide exchange factor (GEF) for Gαi, to serve as a direct platform for multiple RTKs to activate Gαi proteins. Using a combination of homology modeling, protein–protein interaction, and kinase assays, we demonstrate that a stretch of ∼110 amino acids within GIV C-terminus displays structural plasticity that allows folding into a SH2-like domain in the presence of phosphotyrosine ligands. Using protein–protein interaction assays, we demonstrated that both SH2 and GEF domains of GIV are required for the formation of a ligand-activated ternary complex between GIV, Gαi, and growth factor receptors and for activation of Gαi after growth factor stimulation. Expression of a SH2-deficient GIV mutant (Arg 1745→Leu) that cannot bind RTKs impaired all previously demonstrated functions of GIV—Akt enhancement, actin remodeling, and cell migration. The mechanistic and structural insights gained here shed light on the long-standing questions surrounding RTK/G protein cross-talk, set a novel paradigm, and characterize a unique pharmacological target for uncoupling GIV-dependent signaling downstream of multiple oncogenic RTKs.

Protein–protein interaction analysis using an affinity peptide tag and hydrophilic polystyrene plate

2007 ◽  
Vol 128 (2) ◽  
pp. 354-361 ◽  
Author(s):  
Y KUMADA ◽  
C ZHAO ◽  
R ISHIMURA ◽  
H IMANAKA ◽  
K IMAMURA ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Interaction Analysis ◽  
Protein Protein Interaction ◽  
Polystyrene Plate ◽  
Affinity Peptide ◽  
Peptide Tag

scholarly journals Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization

2008 ◽  
Vol 5 (6) ◽  
pp. 561-567 ◽  
Author(s):  
Damien Maurel ◽  
Laëtitia Comps-Agrar ◽  
Carsten Brock ◽  
Marie-Laure Rives ◽  
Emmanuel Bourrier ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protein Interaction ◽  
Interaction Analysis ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Time Resolved ◽  
Protein Protein Interaction
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