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|Title:||Keeping IGF-II under control: Lessons from the IGF-II-IGF2R crystal structure|
|Citation:||Trends in Biochemical Sciences, 2009; 34(12):612-619|
|Publisher:||Elsevier Science London|
|James Brown, E. Yvonne Jones and Briony E. Forbes|
|Abstract:||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 (IGF-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.|
Insulin-Like Growth Factor II
Receptor, IGF Type 2
Protein Structure, Secondary
Protein Structure, Tertiary
|Appears in Collections:||Aurora harvest|
Molecular and Biomedical Science publications
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