期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 34, 期 12, 页码 612-619出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2009.07.003
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资金
- Cancer Research UK [10976] Funding Source: researchfish
- Cancer Research UK [10976] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Insulin-like growth factor-II (IGF-II) is a key regulator of cell growth, survival, migration and differentiation. Its pivotal role in these processes requires tight regulation of both expression and activity. The type 1 IGF receptor tyrosine kinase (IGIF-1R) mediates IGF-II actions, and a family of six high affinity IGF binding proteins (IGFBPs) regulates IGF-II circulating half-life and its availability to bind IGF-1R. In addition, the type 2 IGF receptor (IGF2R; also called the cation-independent mannose-6-phosphate receptor) modulates the circulating and tissue levels of IGF-II by targeting it to lysosomes for degradation. The recently elucidated crystal structure of IGFII-IGF2R complex provides new insight into IGF-II regulation, and reveals a common binding surface on IGF-II for the regulatory proteins, IGF2R and the IGFBPs.
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