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Vol. 14, Issue 11, 4676-4684, November 2003

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Receptor Internalization in Yeast Requires the Tor2-Rho1 Signaling Pathway

Amy K.A. deHart, Joshua D. Schnell, Damian A. Allen, Ju-Yun Tsai, and Linda Hicke *

Department of Biochemistry, Molecular Biology and Cell Biology Northwestern University, Evanston, Illinois 60208

Submitted May 22, 2003; Revised July 23, 2003; Accepted July 24, 2003
Monitoring Editor: Benjamin Glick

Efficient internalization of proteins from the cell surface is essential for regulating cell growth and differentiation. In a screen for yeast mutants defective in ligand-stimulated internalization of the {alpha}-factor receptor, we identified a mutant allele of TOR2, tor2G2128R. Tor proteins are known to function in translation initiation and nutrient sensing and are required for cell cycle progression through G1. Yeast Tor2 has an additional role in regulating the integrity of the cell wall by activating the Rho1 guanine nucleotide exchange factor Rom2. The endocytic defect in tor2G2128R cells is due to disruption of this Tor2 unique function. Other proteins important for cell integrity, Rom2 and the cell integrity sensor Wsc1, are also required for efficient endocytosis. A rho1 mutant specifically defective in activation of the glucan synthase Fks1/2 does not internalize {alpha}-factor efficiently, and fks1{Delta} cells exhibit a similar phenotype. Removal of the cell wall does not inhibit internalization, suggesting that the function of Rho1 and Fks1 in endocytosis is not through cell wall synthesis or structural integrity. These findings reveal a novel function for the Tor2-Rho1 pathway in controlling endocytosis in yeast, a function that is mediated in part through the plasma membrane protein Fks1.

Abbreviations used: GAP, GTPase activating protein; GEF, guanine nucleotide exchange factor; PI, phosphatidyinositol.

* Corresponding author. E-mail address: l-hicke{at}northwestern.edu.




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