Inhibition of nucleoside diphosphate kinase activity by in vitro phosphorylation by protein kinase CK2 Differential phosphorylation of NDP kinases in HeLa cells in culture

FEBS Letters

Sauane, Moira¹  Issinger, Olaf-G.²  Engel, Matthias³  Passeron, Susana⁴  Biondi, Ricardo M.⁴  Welter, Cornelius³  Jiménez de Asúa, Luis¹ 

[1] Instituto de Investigaciones Bioguímicas, Avda. Patricias Argentinas 435, 1405 Buenos Aires, Argentina;Biokemisk Institut, Odense Universitet, 5230 Odense, Denmark;Institut fur Humangenetik, Universitätskliniken Geb 68, 66421 Homburg, Germany;Cátedra de Microbiologia, Facultad de Agronomia, Universidad de Buenos Aires, CIBYF (CONICET), Avda. San Martin 4453, 1417 Buenos Aires, Argentina

关键词: NDP kinase;    nm23;    Protein kinase CK2;    Enzyme inhibition;    Histidine phosphorylation;    NDPK;    nucleoside diphosphate kinase;    CK2;    protein kinase CK2 (formerly called casein kinase 2);    DMEM;    Dulbecco's modified Eagle's medium;   

DOI  :  10.1016/S0014-5793(96)01299-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Although a number of nucleoside diphosphate kinases (NDPKs) have been reported to act as inhibitors of metastasis or as a transcription factor in mammals, it is not known whether these functions are linked to their enzymatic activity or how this protein is regulated. In this report, we show that in vitro protein kinase CK2 catalyzed phosphorylation of human NDPK A inhibits its enzymatic activity by inhibiting the first step of its ping-pong mechanism of catalysis: its autophosphorylation. Upon in vivo ³²P labeling of HeLa cells, we observed that both human NDPKs, A and B, were autophosphorylated on histidine residues, however, only the B isoform appeared to be serine phosphorylated.

【 授权许可】

Unknown