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Palmitoylcarnitine interferes with interaction between protein kinase C (PKC)βII and its receptor – RACK
Author(s) -
SobiesiakMirska J.,
Nałęcz K. A.
Publication year - 2003
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.85.s2.22_12.x
Subject(s) - protein kinase c , autophosphorylation , palmitoylcarnitine , phosphorylation , serine , marcks , kinase , gene isoform , biology , microbiology and biotechnology , chemistry , biochemistry , protein kinase a , enzyme , gene
Palmitoylcarnitine (Pcar), reported to promote differentiation of neuroblastoma NB‐2a cells, was observed to inhibit activity of PKC by decreasing the ability of binding its activators (phorbol esters) and autophorylation on serine moiety ( Neurochem. Int. 2003, 42 , 45). Two PKC isoforms, β and δ were retarded in the cytoplasm upon exposure to Pcar ( Biochim. Biophys. Res Commun. 2002, 294 , 823). An interaction between PKCβII and its receptor was further studied and it was demonstrated that RACK forms much more stable complex with PKCβII in the absence of ATP, an interaction which was shown to be decreased by Pcar. Pcar also diminished colocalisation of βII and RACK at the plasma membrane. In the presence of ATP, under conditions not affecting phosphorylation on threonine, the amount of RACK in a complex with PKCβII was not changed by Pcar, indicating that the first two phosphorylations are sufficient for the complex formation.