| Literature DB >> 14743217 |
Charles Yeaman1, M Inmaculada Ayala, Jessica R Wright, Frederic Bard, Carine Bossard, Agnes Ang, Yusuke Maeda, Thomas Seufferlein, Ira Mellman, W James Nelson, Vivek Malhotra.
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.Entities:
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Year: 2004 PMID: 14743217 PMCID: PMC3372901 DOI: 10.1038/ncb1090
Source DB: PubMed Journal: Nat Cell Biol ISSN: 1465-7392 Impact factor: 28.824