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N‐terminal PH domain and C‐terminal auto‐inhibitory region of CKIP‐1 coordinate to determine its nucleus‐plasma membrane shuttling
Author(s) -
Xi Shenli,
Tie Yi,
Lu Kefeng,
Zhang Minghua,
Yin Xiushan,
Chen Jie,
Xing Guichun,
Tian Chunyan,
Zheng Xiaofei,
He Fuchu,
Zhang Lingqiang
Publication year - 2010
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/j.febslet.2010.02.036
Subject(s) - pleckstrin homology domain , microbiology and biotechnology , nucleus , subcellular localization , c terminus , nuclear localization sequence , casein kinase 2 , biophysics , protein subcellular localization prediction , cytosol , biology , transport protein , chemistry , biochemistry , signal transduction , kinase , protein kinase a , amino acid , cytoplasm , mitogen activated protein kinase kinase , gene , enzyme
The pleckstrin homology (PH) domain‐containing protein casein kinase 2 interacting protein‐1 (CKIP‐1) plays an important role in regulation of bone formation and muscle differentiation. How CKIP‐1 localization is determined remains largely unclear. We observed that isolated CKIP‐1‐PH domain was predominantly localized in the nucleus and the C‐terminus of CKIP‐1 counteracted its nuclear localization. The net charge of basic residues and a serine‐rich motif within the PH domain plays a pivotal role in the localization switch of both full‐length CKIP‐1 and the isolated PH domain. We propose that the N‐terminal PH domain and C‐terminal auto‐inhibitory region of CKIP‐1 coordinate to determine its subcellular localization and the nucleus–plasma membrane shuttling.