Journal article
Protein kinase D regulates basolateral membrane protein exit from trans -Golgi network
Nature cell biology, Vol.6(2), pp.106-112
02/2004
DOI: 10.1038/ncb1090
PMCID: PMC3372901
PMID: 14743217
Abstract
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.
Details
- Title: Subtitle
- Protein kinase D regulates basolateral membrane protein exit from trans -Golgi network
- Creators
- Vivek Malhotra - Cell and Developmental Biology, University of California San DiegoM. Inmaculada Ayala - Cell and Developmental Biology, University of California San DiegoCarine Bossard - Cell and Developmental Biology, University of California San DiegoCharles Yeaman - Department of Anatomy and Cell Biology, University of Iowa Department of Molecular and Cellular Physiology, Stanford University School of MedicineAgnes Ang - Department of Cell Biology, Yale UniversityJessica R Wright - Department of Molecular and Cellular Physiology, Stanford University School of MedicineW. James Nelson - Department of Molecular and Cellular Physiology, Stanford University School of MedicineThomas Seufferlein - Department of Internal Medicine I, University of UlmIra Mellman - Department of Cell Biology, Yale UniversityFrederic Bard - Cell and Developmental Biology, University of California San DiegoYusuke Maeda - Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University
- Resource Type
- Journal article
- Publication Details
- Nature cell biology, Vol.6(2), pp.106-112
- DOI
- 10.1038/ncb1090
- PMID
- 14743217
- PMCID
- PMC3372901
- NLM abbreviation
- Nat Cell Biol
- ISSN
- 1465-7392
- eISSN
- 1476-4679
- Language
- English
- Date published
- 02/2004
- Academic Unit
- Anatomy and Cell Biology; Internal Medicine
- Record Identifier
- 9984025342402771
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