Journal
AGEING RESEARCH REVIEWS
Volume 12, Issue 1, Pages 276-281Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.arr.2012.07.002
Keywords
CKIP-1; PH domain; Localization; Interacting protein; Bone formation; Osteoporosis
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Funding
- National Basic Research Programs [2012CB518103, 2012CB910304, 2011CB910602]
- National Natural Science Foundations of China [31100554, 31125010, 30830029]
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The PH domain-containing casein kinase 2 interacting protein-1 (CKIP-1, also known as PLEKHO1) acts as a scaffold protein mediating interactions with multiple proteins, including CK2 alpha, CP alpha, AP-1/c-Jun, Akt, ATM, IFP35/Nmi and Smurf1. CKIP-1 functions through different ways, such as plasma membrane recruitment, transcriptional activity modulation and posttranscriptional modification regulation. Moreover, the subcellular localization of CKIP-1 is determined by several key amino acids in a cell type dependent style, and the nucleus/plasma membrane shuttle of CKIP-1 is regulated by different cell stresses. As an adaptor protein, CKIP-1 is involved in various important signaling pathways, controlling cell growth, apoptosis, differentiation, cytoskeleton and bone formation. Strikingly, CKIP-1 has been recently demonstrated to be a promising target for treatment of osteoporosis in rat models. In addition, more evidences suggest that CKIP-1 might also function as a potential tumor suppressor. (c) 2012 Elsevier B.V. All rights reserved.
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