Microtubules and signal transduction.
Although molecular components of signal transduction pathways are rapidly being identified, how elements of these pathways are positioned spatially and how signals traverse the intracellular environment from the cell surface to the nucleus or to other cytoplasmic targets are not well understood. The discovery of signaling molecules that interact with microtubules (MTs), as well as the multiple effects on signaling pathways of drugs that destabilize or hyperstabilize MTs, indicate that MTs are likely to be critical to the spatial organization of signal transduction. MTs themselves are also affected by signaling pathways and this may contribute to the transmission of signals to downstream targets.
Gundersen
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GG
Department of Anatomy and Cell Biology Columbia University 630 West 168th Street New York NY 10032 USA. ggg1@columbia.edu
Cook
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TA
D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D018385:Centrosome / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D053823:Hedgehog Proteins; D019476:Insect Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000502:physiology*; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D051153:Wnt Proteins; D029961:Zebrafish Proteins
D029721:Drosophila Proteins; D053823:Hedgehog Proteins; D019476:Insect Proteins; D008869:Microtubule-Associated Proteins; D011518:Proto-Oncogene Proteins; D051153:Wnt Proteins; D029961:Zebrafish Proteins; C077245:hh protein, Drosophila; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D019204:GTP-Binding Proteins