Open AccessStructural and functional insights into the regulation mechanism of CK2 by IP 6 and the intrinsically disordered protein Nopp140
Author(s) -
WonKyu Lee,
Sang Hyeon Son,
Bong-Suk Jin,
JungHyun Na,
SooYoul Kim,
Kook-Han Kim,
Eunice EunKyeong Kim,
Yeon Gyu Yu,
Hyung Ho Lee
Publication year - 2013
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1304670110
Subject(s) - phosphoprotein , protein subunit , casein kinase 2 , kinase , phosphorylation , biochemistry , microbiology and biotechnology , chemistry , threonine , protein kinase a , biology , cyclin dependent kinase 2 , serine , gene
Significance Structural and functional studies on protein kinase CK2α, which is a ubiquitous kinase that can phosphorylate hundreds of cellular proteins, revealed that CK2α activity is inhibited by Nopp140 and reactivated by IP6 by competitive binding at the substrate recognition site of CK2α. IP6 binds to the lysine-rich cluster of CK2α, and phospho-Ser574 on Nopp140 significantly enhances its interaction with CK2α.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom