Through its F-BAR and RhoGAP domains, Rgd1p acts in different polarized growth processes in budding yeast.
Protein domain architecture can be used to construct supramolecular structures, to carry out specific functions and to mediate signaling in prokaryotic and eukaryotic cells. The Rgd1p protein of budding yeast contains two domains with different functions in the cell: the F-BAR and RhoGAP domains. The F-BAR domain has been shown to interact with membrane phospholipids and is thought to induce or sense membrane curvature. The RhoGAP domain activates the GTP hydrolysis of two Rho GTPases, thereby regulating different cellular pathways. Specific molecular interactions with the F-BAR and RhoGAP domains, cell signaling and interplay between these domains may allow the Rgd1p protein to act in several different biological processes, all of which are required for polarized growth in yeast.
Lefebvre
Fabien
F
Université de Bordeaux; Institut de Biochimie et de Génétique Cellulaires and CNRS; UMR 5095; Bordeaux, France.
Prouzet-Mauléon
Valérie
V
Vieillemard
Aurélie
A
Thoraval
Didier
D
Crouzet
Marc
M
Doignon
François
F
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