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Volume 271, Number 49, Issue of December 6, 1996 pp. 31718-31722
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Unique Phosphorylation of Protein Kinase C- in PC12 Cells Induces Resistance to Translocation and Down-regulation

(Received for publication, July 31, 1996, and in revised form, September 19, 1996)

Andrea Gatti and Phillip J. Robinson ^¶

From the ^¶ Endocrinology Unit, John Hunter Hospital, Hunter Region Mail Centre, New South Wales 2310, Australia and the  Department of Experimental Oncology, European Institute of Oncology, 20141 Milan, Italy

Cell exposure to phorbol ester stimulates translocation and activation of protein kinase C (PKC), ultimately followed by its down-regulation. Upon activation, PKC-, the best studied isotype of the PKC family, undergoes changes in its phosphorylation state. With a two-dimensional immunoblot procedure we have previously shown the existence in PC12 cells of several multiply phosphorylated forms of PKC-, whose number increases in response to phorbol esters (Gatti, A., Wang, X., and Robinson, P. J. (1996) Biochim. Biophys. Acta 1313, 111-118). Using the same experimental system, here we report that besides the predominant pool of 80-kDa PKC- forms that respond to phorbol ester by translocating to the cell membranes and down-regulating, there is a small pool of cytosolic 82-kDa PKC- forms that are characterized by a more acidic pI and by an unique resistance to phorbol ester-mediated translocation and down-regulation. The appearance of similarly slower migrating and more acidic PKC- forms is reproduced upon in vitro autophosphorylation in the presence of phosphatidylserine and phorbol ester, but not in the presence of calcium. These results suggest that site-specific transphosphorylation or autophosphorylation of this kinase may regulate its subcellular localization and susceptibility to down-regulation.

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