N‐terminal PH domain and C‐terminal auto‐inhibitory region of CKIP‐1 coordinate to determine its nucleus‐plasma membrane shuttling
N‐terminal PH domain and C‐terminal auto‐inhibitory region of CKIP‐1 coordinate to determine its nucleus‐plasma membrane shuttling
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DOI：
10.1016/j.febslet.2010.02.036
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发表时间：
2010-03
期刊：
影响因子：
3.5
通讯作者：
S. Xi;Yi Tie;Kefeng Lu;Minghua Zhang;Xiushan Yin;Jie Chen;G. Xing;Chunyan Tian;Xiaofei Zheng;F. He;Lingqiang Zhang
中科院分区：
文献类型：
--
作者：
S. Xi;Yi Tie;Kefeng Lu;Minghua Zhang;Xiushan Yin;Jie Chen;G. Xing;Chunyan Tian;Xiaofei Zheng;F. He;Lingqiang Zhang
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.
