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https://hdl.handle.net/2440/56990
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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 1362-4326 |
Statement of Responsibility: | 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 Humans 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 |
Published version: | http://dx.doi.org/10.1016/j.tibs.2009.07.003 |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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