Hematopoietic lineage cell specific protein 1 associates with and down‐regulates protein kinase CK2

FEBS Letters

Brunati, Anna Maria¹  Pinna, Lorenzo A¹  Donella-Deana, Arianna¹  Sarno, Stefania¹  Ruzzene, Maria¹ 

[1] Dipartimento di Chimica Biologica and Centro per lo Studio delle Biomembrane del CNR, University of Padova, Viale G. Colombo, 335121 Padova, Italy

关键词: Casein kinase-2;    HS1;    Protein kinase CK2;    Transformation;    Plasmon resonance;    HS1;    hematopoietic lineage cell-specific protein;    EDC;    N-ethyl-N′-(3-dimethylaminopropyl)-carbodiimide hydrochloride;    f.l.;    full length;    HBS;    HEPES buffer solution;    NHS;    N-hydroxysuccinimide;    PAGE;    polyacrylamide gel electrophoresis;    SH3;    Src homology 3 domain;    SPR;    surface plasmon resonance;    w.t.;    wild-type;   

DOI  :  10.1016/S0014-5793(99)01409-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The catalytic (α) subunit of protein kinase CK2 and the hematopoietic specific protein 1 (HS1) display opposite effects on Ha-ras induced fibroblast transformation, by enhancing and counteracting it, respectively. Here we show the occurrence of physical association between HS1 and CK2α as judged from both far Western blot and plasmon resonance (BIAcore) analysis. Association of HS1 with CK2α is drastically reduced by the deletion of the HS1 C-terminal region (403–486) containing an SH3 domain. HS1, but not its deletion mutant HS1 Δ324–393, lacking a sequence similar to an acidic stretch of the regulatory β-subunit of CK2, inhibits calmodulin phosphorylation by CK2α. These data indicate that HS1 physically interacts with CK2α and down-regulates its activity by a mechanism similar to the β-subunit.

【 授权许可】

Unknown