Letter abstract
Nature Cell Biology 6, 106 - 112 (2004)
Published online: 25 January 2004 | doi:10.1038/ncb1090
Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network
Charles Yeaman1,3,7, M. Inmaculada Ayala2,7, Jessica R. Wright3, Frederic Bard2, Carine Bossard2, Agnes Ang4, Yusuke Maeda5, Thomas Seufferlein6, Ira Mellman4, W. James Nelson3 & Vivek Malhotra2,7
Protein kinase D (PKD) binds to diacylglycerol (DAG) in the trans-Golgi network (TGN) and is activated by trimeric G-protein subunits 
. This complex then regulates the formation of transport carriers in the TGN that traffic to the plasma membrane in non-polarized cells. Here we report specificity of different PKD isoforms in regulating protein trafficking from the TGN. Kinase-inactive forms of PKD1, PKD2 and PKD3 localize to the TGN in polarized and non-polarized cells. PKD activity is required only for the transport of proteins containing basolateral sorting information, and seems to be cargo specific.
- Department of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242-1109, USA.
- Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093-0347, USA.
- Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5345, USA.
- Department of Cell Biology, Yale University, New Haven, CT 06520-8002, USA.
- Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.
- Department of Internal Medicine I, University of Ulm, 89071 Ulm, Germany.
- These authors contributed equally to this work.
Correspondence to: Vivek Malhotra2,7 e-mail: malhotra@biomail.ucsd.edu
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