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Protein kinase C‐θ is specifically activated in murine erythroleukaemia cells during mitosis
Author(s) -
Passalacqua Mario,
Patrone Mauro,
Sparatore Bianca,
Pedrazzi Marco,
Melloni Edon,
Pontremoli Sandro
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)00729-2
Subject(s) - cyclin dependent kinase 9 , protein kinase a , cyclin dependent kinase 2 , autophosphorylation , biology , microbiology and biotechnology , mitosis , map2k7 , c raf , mitogen activated protein kinase kinase , ask1 , metaphase , map kinase kinase kinase , cyclin dependent kinase 3 , kinase , biochemistry , chromosome , gene
Protein kinase C‐θ is a member of the n‐protein kinase C subfamily that in mitotic cells translocates to centrosomes and kinetochores. Although this kinase is expressed in comparable amounts in murine erythroleukaemia cells during the interphase or metaphase, when localized in the mitotic structures, it selectively phosphorylates a 66 kDa protein, also associated to chromosomes. Moreover, protein kinase C‐θ immunoprecipitated from cells at the metaphase results four times more active in the absence of lipid cofactors as compared with the kinase obtained from cells in the interphase. This activation is accomplished by interaction of protein kinase C‐θ with a protein factor which also promotes an increased auto‐phosphorylation of the kinase. These findings indicate that in the mitotic phase of the cell cycle, protein kinase C‐θ recognizes a protein factor which operates as a positive modulator of the kinase activity in the absence lipids.