mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif

Author:

Baffi Timothy R.12ORCID,Lordén Gema1ORCID,Wozniak Jacob M.123,Feichtner Andreas4ORCID,Yeung Wayland56ORCID,Kornev Alexandr P.1ORCID,King Charles C.1,Del Rio Jason C.12,Limaye Ameya J.7ORCID,Bogomolovas Julius8ORCID,Gould Christine M.12ORCID,Chen Ju8,Kennedy Eileen J.7ORCID,Kannan Natarajan56ORCID,Gonzalez David J.13,Stefan Eduard4ORCID,Taylor Susan S.19ORCID,Newton Alexandra C.1ORCID

Affiliation:

1. Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA.

2. Biomedical Sciences Graduate Program, University of California at San Diego, La Jolla, CA 92093, USA.

3. Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA 92093, USA.

4. Institute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck A-6020, Austria.

5. Institute of Bioinformatics, University of Georgia, Athens, GA 30602, USA.

6. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.

7. Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, University of Georgia, Athens, GA 30602, USA.

8. Department of Medicine, University of California at San Diego, La Jolla, CA 92093, USA.

9. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA 92093, USA.

Abstract

Phosphorylation of an evolutionarily conserved motif by mTORC2 enables the maturation of AGC kinases.

Funder

National Institutes of Health

University of California, San Diego

Austrian Science Fund

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

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