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Type: Journal article
Title: Keeping IGF-II under control: Lessons from the IGF-II-IGF2R crystal structure
Author: Brown, J.
Jones, E.
Forbes, B.
Citation: Trends in Biochemical Sciences, 2009; 34(12):612-619
Publisher: Elsevier Science London
Issue Date: 2009
ISSN: 0968-0004
Statement of
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.
Keywords: Animals
Insulin-Like Growth Factor II
Receptor, IGF Type 2
Binding Sites
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Binding
DOI: 10.1016/j.tibs.2009.07.003
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Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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