G proteins, phosphoinositides, and actin-cytoskeleton in the control of cancer growth.
Almost three decades have passed since actin-cytoskeleton (acto-myosin complex) was first discovered in non-muscle cells. A combination of cell biology, biochemistry, and molecular biology has revealed the structure and function of many actin-binding proteins and their physiological role in the regulation of cell motility, shape, growth, and malignant transformation. As molecular oncologists, we would like to review how the function of actin-cytoskeleton is regulated through Ras/Rho family GTPases- or phosphoinosites-mediated signaling pathways, and how malignant transformation is controlled by actin/phosphoinositides-binding proteins or drugs that block Rho/Rac/CDC42 GTPases-mediated signaling pathways.
Maruta
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H
Ludwig Institute for Cancer Research, Melbourne, Australia 3050. hiroshi.maruta@ludwig.edu.au
He
H
H
Tikoo
A
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Vuong
T
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Nur-E-Kamal
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M
D000199:Actins / Q000502:physiology*; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D003599:Cytoskeleton / Q000737:chemistry*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D020558:GTP Phosphohydrolases / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008840:Microfilament Proteins / Q000502:physiology*; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000502:physiology*; D010716:Phosphatidylinositols / Q000502:physiology; D015398:Signal Transduction / Q000187:drug effects; D018631:ras Proteins / Q000187:drug effects
D000199:Actins; D004791:Enzyme Inhibitors; D008840:Microfilament Proteins; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; D018631:ras Proteins