scholarly journals Correction for Batta and Kundu, “Activation of p53 Function by Human Transcriptional Coactivator PC4: Role of Protein-Protein Interaction, DNA Bending, and Posttranslational Modifications”

2020 ◽  
Vol 40 (19) ◽  
Author(s):  
Kiran Batta ◽  
Tapas K. Kundu
Keyword(s):  
Protein Interaction ◽  
Posttranslational Modifications ◽  
Dna Bending ◽  
Transcriptional Coactivator ◽  
Protein Protein Interaction

scholarly journals Regulation of clathrin coat assembly by Eps15 homology domain–mediated interactions during endocytosis

2012 ◽  
Vol 23 (4) ◽  
pp. 687-700 ◽  
Author(s):  
Ryohei Suzuki ◽  
Junko Y. Toshima ◽  
Jiro Toshima
Keyword(s):  
Functional Diversity ◽  
Protein Interaction ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Molecular Events ◽  
Biological Studies ◽  
Eh Domain ◽  
Actin Patch ◽  
Lines Of Evidence

Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions among a variety of proteins and lipids through specific domains. One such domain is the Eps15 homology (EH) domain, a highly conserved protein–protein interaction domain present in a number of proteins distributed from yeast to mammals. Several lines of evidence suggest that the yeast EH domain–containing proteins Pan1p, End3p, and Ede1p play important roles during endocytosis. Although genetic and cell-biological studies of these proteins suggested a role for the EH domains in clathrin-mediated endocytosis, it was unclear how they regulate clathrin coat assembly. To explore the role of the EH domain in yeast endocytosis, we mutated those of Pan1p, End3p, or Ede1p, respectively, and examined the effects of single, double, or triple mutation on clathrin coat assembly. We found that mutations of the EH domain caused a defect of cargo internalization and a delay of clathrin coat assembly but had no effect on assembly of the actin patch. We also demonstrated functional redundancy among the EH domains of Pan1p, End3p, and Ede1p for endocytosis. Of interest, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

scholarly journals Analysis of origin and protein-protein interaction maps suggests distinct oncogenic role of nuclear EGFR during cancer evolution

2017 ◽  
Vol 8 (5) ◽  
pp. 903-912 ◽  
Author(s):  
Ainur Sharip ◽  
Diyora Abdukhakimova ◽  
Xiao Wang ◽  
Alexey Kim ◽  
Yevgeniy Kim ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Cancer Evolution ◽  
Protein Protein Interaction

scholarly journals VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83

Microbiology ◽  
2006 ◽  
Vol 152 (11) ◽  
pp. 3383-3389 ◽  
Author(s):  
E. Vanterpool ◽  
F. Roy ◽  
W. Zhan ◽  
S. M. Sheets ◽  
L. Sangberg ◽  
...  
Keyword(s):  
Gene Product ◽  
Porphyromonas Gingivalis ◽  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Studies ◽  
Defective Mutant ◽  
Protease Activation ◽  
Porphyromonas Gingivalis W83

The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein–protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.

On the role of lipid-bilayer elasticity for the lipid–protein interaction and the indirect protein–protein coupling

1984 ◽  
Vol 62 (8) ◽  
pp. 778-788 ◽  
Author(s):  
E. Sackmann ◽  
R. Kotulla ◽  
Franz-Josef Heiszler
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Protein Interaction ◽  
Experimental Studies ◽  
Membrane Elasticity ◽  
Protein Protein Interaction ◽  
Lipid Protein Interaction ◽  
Elastic Distortion ◽  
Enzyme Complexes

The present paper deals with the curvature (or splay) elasticity of lipid bilayers and its possible consequences for the microscopic organization of membranes. Experimental studies of the microstructure of lipid–lipid and lipid–protein mixtures are reported and discussed in terms of this type of membrane elasticity. In particular, evidence is provided that the elastic distortion of lipid bilayers caused by the incorporation of proteins can lead to mechanisms of the indirect protein–protein interaction. Finally the question is discussed whether these mechanisms could also play a role for the formation of enzyme complexes in biological membranes.

Protein kinases in seeds

1998 ◽  
Vol 8 (2) ◽  
pp. 193-200 ◽  
Author(s):  
M. K. Walker-Simmons
Keyword(s):  
Amino Acid ◽  
Environmental Stress ◽  
Protein Phosphorylation ◽  
Protein Kinases ◽  
Protein Interaction ◽  
Stress Responses ◽  
Amino Acid Residues ◽  
Protein Protein Interaction ◽  
Reversible Protein Phosphorylation

AbstractReversible phosphorylation is catalysed by protein kinases that transfer the γ-phosphate from ATP to amino acid residues of proteins. The process can be reversed by protein phosphatases. Phosphorylation can dramatically activate or inhibit enzymes and affect protein-protein interaction. Through phosphorylation protein kinases can amplify and propagate cellular signals. In plants and now seeds, protein kinases involved in hormone, defence and environmental stress responses are being identified. Increasingly, these protein kinases are being cloned and characterized, demonstrating the major role of reversible protein phosphorylation in seeds.

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