Protein machines and self assembly in muscle organization

Article Abstract:

Author's Abstract: COPYRIGHT 1999, John Wiley & Sons, Inc. The remarkable order of striated muscle is the result of a complex series of protein interactions at different levels of organization. Within muscle, the thick filament and its major protein myosin are classical examples of functioning protein machines. Our understanding of the structure and assembly of thick filaments and their organization into the regular arrays of the A-band has recently been enhanced by the applicaiton of biochemical, genetic, and structural approaches. Detailed studies of the thick filament backbone have shown that the myosins are organized into a tubular structure. Additional protein machines and specific myosin rod sequences have been identified that play significant roles in thick filament structure, assembly, and organization. These include intrinsic filament components, cross-linking molecules of the M-band and constituents of the membrane-cytoskeleton system. Muscle organization is directed by the multistep actions of protein machines that take advantage of well-established self-assembly relationships.

Physiological aspects, Muscles, Muscle proteins, Myosin

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AMP-activated protein kinase - an archetypal protein kinase cascade?

Article Abstract:

Mammalian AMP-activated protein kinase inactivates acetyl-CoA carboxylase, HMG-CoA reductase and hormone-sensitive lipase/cholesterol esterase, all of which are involved in the synthesis and intracellular release of free fatty acids and cholesterol. This protein kinase cascade system performs a protective function in a type of stress response, and is also widely distributed among higher plants which suggest that it has been in existence for at least a billion years. Moreover, intracellular metabolites rather than extracellular signals and cell cycle events regulate the system.

Protein kinases, Lipids, Lipid synthesis

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The trick of the tail: Protein-protein interactions of metabotropic glutamate receptors

Article Abstract:

The proteins interacting with metabotropic glutamate receptor (mGluR) C-termini are identified and characterized. The analysis has highlighted the new evolving regulatory mechanisms for glutamatergic signal transduction and drug development.

Science & research, Glutamate, G proteins, Protein-protein interactions

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