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Molecular and Cellular Biology, January 2009, p. 435-447, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01144-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Identification of G Protein {alpha} Subunit-Palmitoylating Enzyme{triangledown}

Ryouhei Tsutsumi,1 Yuko Fukata,1,2 Jun Noritake,1 Tsuyoshi Iwanaga,1 Franck Perez,3,4 and Masaki Fukata1,2*

Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, Okazaki, Aichi 444-8787, Japan,1 PRESTO, Japan Science and Technology Agency, Chiyoda, Tokyo 102-0075, Japan,2 Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144,3 Institut Curie Section Recherche, 75248 Paris Cedex 05, France4

Received 20 July 2008/ Returned for modification 14 August 2008/ Accepted 29 October 2008

The heterotrimeric G protein {alpha} subunit (G{alpha}) is targeted to the cytoplasmic face of the plasma membrane through reversible lipid palmitoylation and relays signals from G-protein-coupled receptors (GPCRs) to its effectors. By screening 23 DHHC motif (Asp-His-His-Cys) palmitoyl acyl-transferases, we identified DHHC3 and DHHC7 as G{alpha} palmitoylating enzymes. DHHC3 and DHHC7 robustly palmitoylated G{alpha}q, G{alpha}s, and G{alpha}i2 in HEK293T cells. Knockdown of DHHC3 and DHHC7 decreased G{alpha}q/11 palmitoylation and relocalized it from the plasma membrane into the cytoplasm. Photoconversion analysis revealed that G{alpha}q rapidly shuttles between the plasma membrane and the Golgi apparatus, where DHHC3 specifically localizes. Fluorescence recovery after photobleaching studies showed that DHHC3 and DHHC7 are necessary for this continuous G{alpha}q shuttling. Furthermore, DHHC3 and DHHC7 knockdown blocked the {alpha}1A-adrenergic receptor/G{alpha}q/11-mediated signaling pathway. Together, our findings revealed that DHHC3 and DHHC7 regulate GPCR-mediated signal transduction by controlling G{alpha} localization to the plasma membrane.

* Corresponding author. Mailing address: Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan. Phone: 81 564 59 5873. Fax: 81 564 59 5870. E-mail: mfukata{at}nips.ac.jp

{triangledown} Published ahead of print on 10 November 2008.

Molecular and Cellular Biology, January 2009, p. 435-447, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01144-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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