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Molecular and Cellular Biology, August 2005, p. 7239-7248, Vol. 25, No. 16
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.16.7239-7248.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Tor2 Directly Phosphorylates the AGC Kinase Ypk2 To Regulate Actin Polarization{dagger}

Yoshiaki Kamada,1,2* Yuko Fujioka,3 Nobuo N. Suzuki,3 Fuyuhiko Inagaki,3 Stephan Wullschleger,4 Robbie Loewith,4,{ddagger} Michael N. Hall,4 and Yoshinori Ohsumi1

Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan,1 CREST, Japan Science and Technology Agency, Kawaguchi 332-0012, Japan,2 Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan,3 Division of Biochemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland4

Received 6 January 2005/ Returned for modification 8 March 2005/ Accepted 25 May 2005

The target of rapamycin (TOR) protein kinases, Tor1 and Tor2, form two distinct complexes (TOR complex 1 and 2) in the yeast Saccharomyces cerevisiae. TOR complex 2 (TORC2) contains Tor2 but not Tor1 and controls polarity of the actin cytoskeleton via the Rho1/Pkc1/MAPK cell integrity cascade. Substrates of TORC2 and how TORC2 regulates the cell integrity pathway are not well understood. Screening for multicopy suppressors of tor2, we obtained a plasmid expressing an N-terminally truncated Ypk2 protein kinase. This truncation appears to partially disrupt an autoinhibitory domain in Ypk2, and a point mutation in this region (Ypk2D239A) conferred upon full-length Ypk2 the ability to rescue growth of cells compromised in TORC2, but not TORC1, function. YPK2D239A also suppressed the lethality of tor2{Delta} cells, suggesting that Ypks play an essential role in TORC2 signaling. Ypk2 is phosphorylated directly by Tor2 in vitro, and Ypk2 activity is largely reduced in tor2{Delta} cells. In contrast, Ypk2D239A has increased and TOR2-independent activity in vivo. Thus, we propose that Ypk protein kinases are direct and essential targets of TORC2, coupling TORC2 to the cell integrity cascade.

* Corresponding author. Mailing address: Department of Cell Biology, National Institute for Basic Biology, Maiodaiji-Cho, Okazaki 444-8585, Japan. Phone: 81-564-55-7517. Fax: 81-564-55-7516. E-mail: yoshikam{at}nibb.ac.jp.

{dagger} This paper is dedicated to the memory of Shoshi Muto, whose mentorship meant a great deal to Y.K.

{ddagger} Present address: Department of Molecular Biology, Sciences III, 30, Quai Ernest-Ansermet, CH-1211, Geneva 4, Switzerland.

Molecular and Cellular Biology, August 2005, p. 7239-7248, Vol. 25, No. 16
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.16.7239-7248.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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