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  • 1
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    MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Baoxue -- Gram, Hermann -- Di Padova, Franco -- Huang, Betty -- New, Liguo -- Ulevitch, Richard J -- Luo, Ying -- Han, Jiahuai -- AI41637/AI/NIAID NIH HHS/ -- HL07195/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847341" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; *Drosophila Proteins ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Imidazoles/pharmacology ; *Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase 6 ; *MAP Kinase Signaling System ; Membrane Glycoproteins/metabolism ; Mitogen-Activated Protein Kinase 14 ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Mutation ; Peptide Mapping ; Peroxynitrous Acid/pharmacology ; Phosphorylation ; Proteins/metabolism ; Pyridines/pharmacology ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 6 ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/pharmacology ; Two-Hybrid System Techniques ; p38 Mitogen-Activated Protein Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Evolutionary Cell Computing: From Protocells to Self-Organized Computing (2000)
    In:  CASI
    Details
    Publication Date: 2017-10-04
    Description: On the path from inanimate to animate matter, a key step was the self-organization of molecules into protocells - the earliest ancestors of contemporary cells. Studies of the properties of protocells and the mechanisms by which they maintained themselves and reproduced are an important part of astrobiology. These studies also have the potential to greatly impact research in nanotechnology and computer science. Previous studies of protocells have focussed on self-replication. In these systems, Darwinian evolution occurs through a series of small alterations to functional molecules whose identities are stored. Protocells, however, may have been incapable of such storage. We hypothesize that under such conditions, the replication of functions and their interrelationships, rather than the precise identities of the functional molecules, is sufficient for survival and evolution. This process is called non-genomic evolution. Recent breakthroughs in experimental protein chemistry have opened the gates for experimental tests of non-genomic evolution. On the basis of these achievements, we have developed a stochastic model for examining the evolutionary potential of non-genomic systems. In this model, the formation and destruction (hydrolysis) of bonds joining amino acids in proteins occur through catalyzed, albeit possibly inefficient, pathways. Each protein can act as a substrate for polymerization or hydrolysis, or as a catalyst of these chemical reactions. When a protein is hydrolyzed to form two new proteins, or two proteins are joined into a single protein, the catalytic abilities of the product proteins are related to the catalytic abilities of the reactants. We will demonstrate that the catalytic capabilities of such a system can increase. Its evolutionary potential is dependent upon the competition between the formation of bond-forming and bond-cutting catalysts. The degree to which hydrolysis preferentially affects bonds in less efficient, and therefore less well-ordered, peptides is also critical to evolution of a non-genomic system. Based on these results, a new computational object called a "molnet" is defined. Like a neural network, it is formed of interconnected units that send "signals" to each other. Like molecules, neural networks have a specific function once their structure is defined. The difference between a molnet and traditional neural networks, is that input to molnets is not simply passed along and processed from input to output units, but rather it is utilized to form and break connections(bonds), and thus to form new structures. Molnets represent a powerful tool that can be used to understand the conditions under which chemical systems can form large molecules, such as proteins, and display ever more complex functions. This has direct applications, for example to the design of smart,synthetic fabrics. Additional information is contained in the original.
    Keywords: Computer Programming and Software
    Format: text
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