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J. Biol. Chem., Vol. 278, Issue 3, 1991-1997, January 17, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/3/1991    most recent M209982200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Birkeli, K. A. Articles by Sandvig, K. Search for Related Content PubMed PubMed Citation Articles by Birkeli, K. A. Articles by Sandvig, K. Social Bookmarking                      What's this?

Endosome-to-Golgi Transport Is Regulated by Protein Kinase A Type II^*

Kim Are Birkeli, Alicia Llorente, Maria L. Torgersen, Guy Keryer^§, Kjetil Taskén^¶, and Kirsten Sandvig

From the  Institute for Cancer Research, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway, ^§ Institut Curie, Biologie du Cycle Cellulaire et de la Motilité, 75248 Paris Cedex 05, France, and the ^¶ Institute of Medical Biochemistry, University of Oslo, 0317 Oslo, Norway

Studies of RII-deficient B lymphoid cells and stable transfectants expressing the type II regulatory subunit (RII) of cAMP-dependent protein kinase (PKA), which is targeted to the Golgi-centrosomal area, reveal that the presence of a Golgi-associated pool of PKA type II mediates a change in intracellular transport of the plant toxin ricin. The transport of ricin from endosomes to the Golgi apparatus, measured as sulfation of a modified ricin (ricin sulf-1), increased in RII-expressing cells when PKA was activated. However, not only endosome-to-Golgi transport, but also retrograde ricin transport to the endoplasmic reticulum (ER), measured as sulfation and N-glycosylation of another modified ricin (ricin sulf-2), seemed to be increased in cells expressing RII in the presence of a cAMP analog, 8-(4-chlorophenylthio)-cAMP. Thus, PKA type II seems to be involved in both endosome-to-Golgi and Golgi-to-ER transport. Because ricin, after being retrogradely transported to the ER, is translocated to the cytosol, where it inhibits protein synthesis, we also investigated the influence of RII expression on ricin toxicity. In agreement with the other data obtained, 8-(4-chlorophenylthio)-cAMP and RII were found to sensitize cells to ricin, indicating an increased transport of ricin to the cytosol. In conclusion, our results demonstrate that transport of ricin from endosomes to the Golgi apparatus and further to the ER is regulated by PKA type II isozyme.

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