By J. Silvio Gutkind
Top scientists summarize the newest findings on sign transduction and mobilephone cycle rules and describe the trouble to layout and synthesize inhibiting molecules, in addition to to judge their biochemical and organic actions. They evaluation the proper mobile floor receptors, their ligands, and their downstream pathways. additionally tested are the newest findings at the elements of novel signaling networks controlling the task of nuclear transcription components and phone cycle regulatory molecules. state of the art and hugely suggestive, Signaling Networks and phone Cycle regulate: The Molecular foundation of melanoma and different ailments offers a wealth of data at the rising rules of the sector, in addition to a useful advisor for all experimental and scientific investigators of mobile rules and its speedily rising pharmacological possibilities this day.
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Extra resources for Signaling networks and cell cycle control: the molecular basis of cancer and other diseases
In vitro substrates of FAK appear to include paxillin and tensin; the biological sequelae of this enhancement in vivo remain to be established. The clearest biological effect of FAK is to enhance rates of cell migration, as shown by the opposing effects of gene ablation and overexpression (6668). The ability of FAK to accelerate integrin-dependent migration requires the autophosphorylation site Y397, to which c-Src can bind after phosphorylation. Conversely, FAK-null (knockout) mice die with defects in gastrulation at about the same time in development as fibronectin-deficient mice; cells from these mice show defective rates of migration (66,69).
In addition, FAK becomes phosphorylated on tyrosine residues. This process does not require integrin ligand occupancy, but only integrin clustering. , by binding to intact fibronectin; see ref. 31 and citations therein). Although the consequences of simple integrin occupancy without clustering generally appear quite limited in terms of signaling, an interesting exception occurs in certain embryonic cells. Interactions of isolated segmental plate or of neural crest cells with peptides containing the Arg-Gly-Asp integrin-binding motif results in a strong induction of cell-cell adhesion that is dependent on N-cadherin (43,44).
M. Yamada, unpublished data). Integrin b cytoplasmic tails also contain sufficient information to induce the physical localization of single-subunit chimeras to pre-existing focal contacts, presumably by binding to cytoskeletal components enriched at these sites (24). This property may contribute to the organization of integrins into adhesion complexes. Although a cytoplasmic domains lack such direct activities, analyses using chimeras demonstrate that a tails can have strikingly distinct effects on cell adhesion, migration, growth, and differentiation (25,26).