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Published online December 17, 2007
doi:10.1083/jcb.200703166
The Journal of Cell Biology, Vol. 179, No. 6, 1123-1131
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Bossard et al.
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Dimeric PKD regulates membrane fission to form transport carriers at the TGN



Carine Bossard1, Damien Bresson2, Roman S. Polishchuk3, and Vivek Malhotra1

1 Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093
2 La Jolla Institute for Allergy and Immunology, Developmental Immunology 3, La Jolla, CA 92037
3 Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro (CH) 66030, Italy

Correspondence to Vivek Malhotra: vivek.malhotra{at}crg.es

Protein kinase D (PKD) is recruited to the trans-Golgi network (TGN) through interaction with diacylglycerol (DAG) and is required for the biogenesis of TGN to cell surface transport carriers. We now provide definitive evidence that PKD has a function in membrane fission. PKD depletion by siRNA inhibits trafficking from the TGN, whereas expression of a constitutively active PKD converts TGN into small vesicles. These findings demonstrate that PKD regulates membrane fission and this activity is used to control the size of transport carriers, and to prevent uncontrolled vesiculation of TGN during protein transport.

V. Malhotra's present address is Cell and Developmental Biology program, Centre de Regulació Genòmica (CRG), Dr. Aiguader 88, 08003 Barcelona, Spain.

Abbreviations used in this paper: CA, constitutively active; KD, kinase dead; PKD, protein kinase D; PLAP, placental alkaline phosphatase; SS, signal sequence; ST, sialyltransferase.


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