A flip-flop switch in polarity signaling.
The Rho GTPase Cdc42 is essential for polarized growth of budding yeast. Temporal control of Cdc42 depends partly on the activity of its GTPase-activating proteins (GAPs). In this issue of Developmental Cell, Saito et al. report that Cdc42 GAP activity is regulated by the phospholipid composition of the bud-tip membrane, under control of the phospholipid flippases Lem3-Dnf1 and Lem3-Dnf2.
Menon
Anant K
AK
Department of Biochemistry, Weill Cornell Medical College, 1300 York Avenue, New York, NY 10065, USA. Electronic address: akm2003@med.cornell.edu.
D018528:ATP-Binding Cassette Transporters; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity; D026901:Membrane Transport Proteins / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D020764:cdc42 GTP-Binding Protein / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; C478771:Lem3 protein, S cerevisiae; D026901:Membrane Transport Proteins; D010743:Phospholipids; D029701:Saccharomyces cerevisiae Proteins; D000251:Adenosine Triphosphatases; C480602:Dnf2 protein, S cerevisiae; D020764:cdc42 GTP-Binding Protein; C480601:Dnf1 protein, S cerevisiae