A big new job for small GTPases.
Members of the Ras superfamily of small guanosine triphosphatases (GTPases) function as key nodes within signaling networks in a remarkable range of cellular processes, including cell proliferation, differentiation, growth, cell-cell adhesion and apoptosis. We recently described a novel role for the Ras-like small GTPases Rap1 and Ral in regulating cortical polarity and spindle orientation during asymmetric neuroblast division in Drosophila. The participation of these proteins in promoting cell polarization seems to be a common theme throughout evolution.
Instituto de Neurociencias, CSIC/UMH, 03550-Sant Joan d'Alacant, Alicante, Spain. acarmena@umh.es
Ana
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Carmena
D000818:Animals; D016764:Cell Polarity; D004330:Drosophila / Q000166:cytology / Q000378:metabolism; D029721:Drosophila Proteins / Q000378:metabolism; D006801:Humans; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D015398:Signal Transduction; D020725:ral GTP-Binding Proteins / Q000378:metabolism; D020827:rap1 GTP-Binding Proteins / Q000378:metabolism
D029721:Drosophila Proteins; D029701:Saccharomyces cerevisiae Proteins; D020559:Monomeric GTP-Binding Proteins; D020725:ral GTP-Binding Proteins; D020827:rap1 GTP-Binding Proteins