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Comparison of the roles of the C1a and C1b domains of protein kinase C alpha in ligand induced translocation in NIH 3T3 cells
Author(s) -
Bögi K.,
Lorenzo P.S.,
Ács P.,
Szállási Z.,
Wagner G.S.,
Blumberg P.M.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00927-8
Subject(s) - protein kinase c , chromosomal translocation , gene isoform , phorbol , 3t3 cells , microbiology and biotechnology , phorbol ester , alpha (finance) , chemistry , kinase , biology , biochemistry , gene , transfection , medicine , construct validity , nursing , patient satisfaction
To explore the relative roles of the two C1 domains of protein kinase C alpha (PKCα) in the response to phorbol esters and related analogs, we mutated the individual C1 domains, expressed the mutated PKCα in NIH 3T3 cells, and then examined the ability of ligands to induce its translocation to the membrane. The C1a and C1b domains play equivalent roles for translocation in response to phorbol 12‐myristate 13‐acetate, mezerein, and (−)octylindolactam V. These results contrast with those previously reported for PKCδ, suggesting that the domains play different roles in different PKC isoforms.