Signal transduction regulatory proteins

The signal transduction G-proteins or heterotrimeric GTP binding proteins, are interposed between cell siuface receptors and intracellular effectors. The signal tran uction G-proteins are a family of GTP-binding proteins in which the GTP-GDP switch serves to propagate and amplify regulatory signals from activated cellular membrane receptors to effector channels and enemies. 

Calculation of Conformational Free Energies for a Model of a Bilobal Enzyme Protein kinases catalyze the transfer of phosphate from adenosine triphosphate (ATP) to protein substrates and are regulatory elements of most known pathways of signal transduction. 

The smooth muscle cell does not respond in an all-or-none manner, but instead its contractile state is a variable compromise between diverse regulatory influences. While a vertebrate skeletal muscle fiber is at complete rest unless activated by a motor nerve, regulation of the contractile activity of a smooth muscle cell is more complex. First, the smooth muscle cell typically receives input from many different kinds of nerve fibers. The various cell membrane receptors in turn activate different intracellular signal-transduction pathways which may affect (a) membrane channels, and hence, electrical activity (b) calcium storage or release or (c) the proteins of the contractile machinery. While each have their own biochemically specific ways, the actual mechanisms are for the most part known only in outline. 

Nucleotides participate in reactions that fulfill physiologic functions as diverse as protein synthesis, nucleic acid synthesis, regulatory cascades, and signal transduction pathways. 

Fig. 1. The generalized protein-protein interaction network that includes (A) direct protein-protein interactions such as in the signal transduction pathway, (B) enzyme-enzyme relations in the metabolic pathway, and (C) transcription factor-expressed gene product relations in the gene regulatory pathway. The interactions in (B) and (C) are termed indirect protein-protein interactions.

Figure 3.14 Model of H2-dependent signal transduction in R. eutropha. Proteins which are regulatory active are highlighted in black. For details, see text.

Action. cAMP is an allosteric effector of protein kinase A (PK-A, [3]). in the inactive state, PK-A is a heterotetramer (C2R2), the catalytic subunits of which (C) are blocked by regulatory units (R autoinhibition). When cAMP binds to the regulatory units, the C units separate from the R units and become enzymatically active. Active PK-A phosphorylates serine and threonine residues of more than 100 different proteins, enzymes, and transcription factors, in addition to cAMP, cCMP also acts as a second messenger, it is involved in sight (see p. 358) and in the signal transduction of NO (see p. 388). 

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