Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network

Nat Cell Biol. 2004 Feb;6(2):106-12. doi: 10.1038/ncb1090.

Charles Yeaman ¹, M Inmaculada Ayala, Jessica R Wright, Frederic Bard, Carine Bossard, Agnes Ang, Yusuke Maeda, Thomas Seufferlein, Ira Mellman, W James Nelson, Vivek Malhotra

Affiliations

Affiliation

1 Department of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242-1109, USA.

PMID: 14743217 DOI: 10.1038/ncb1090

Abstract

Protein kinase D (PKD) binds to diacylglycerol (DAG) in the trans-Golgi network (TGN) and is activated by trimeric G-protein subunits beta gamma. 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.

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