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

被引：0
作者：
Charles Yeaman
M. Inmaculada Ayala
Jessica R. Wright
Frederic Bard
Carine Bossard
Agnes Ang
Yusuke Maeda
Thomas Seufferlein
Ira Mellman
W. James Nelson
Vivek Malhotra
机构：
[1] University of Iowa,Department of Anatomy and Cell Biology
[2] Cell and Developmental Biology,Department of Molecular and Cellular Physiology
[3] University of California San Diego,Department of Cell Biology
[4] Stanford University School of Medicine,Department of Immunoregulation
[5] Yale University,Department of Internal Medicine I
[6] Research Institute for Microbial Diseases,undefined
[7] Osaka University,undefined
[8] University of Ulm,undefined
来源：
Nature Cell Biology | 2004年 / 6卷
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摘要：
Protein kinase D (PKD) binds to diacylglycerol (DAG) in the trans-Golgi network (TGN) and is activated by trimeric G-protein subunits βγ. 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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页码：106 / 112
页数：6
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