Cysteine cross-linking analysis reveals new insights into growth factor receptor signalling.

Growth factors and their receptors are central in directing cell division, development and differentiation. Their role in controlling cell fate makes them one of the most hijacked protein classes during cancer formation, leading many of the receptors to being termed tumorigenic receptors. Thus as a family of receptors, they have become one of the major targets of therapeutic intervention for cancer therapy. 

Growth factor receptors are often Cysteine rich transmembrane proteins that bind specific growth factors and transmit instructions by these factors through the plasma membrane, activating intracellular signalling cascades. Here, Xu et al, combines the use of cutting-edge Cryo-Electron microscopy with deep cysteine cross-linking analyse using IonOpticks based mass spectrometry to provide a deeper understanding of the mechanism of signal transduction that may one day lead to better small molecule therapeutics.

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How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor.

Structure. 2020 May 26:S0969-2126(20)30171-4. doi: https://doi.org/10.1016/j.str.2020.05.002
Xu Y, Kirk NS, Venugopal H, Margetts MB, Croll TI, Sandow JJ, Webb AI, Delaine CA, Forbes BE, Lawrence MC

Commentary by Andrew Webb, PhD.

About the author
Andrew has over 15 years’ experience in the field of chromatography and mass spectrometry. He is the lead innovator and inventor at IonOpticks, working closely with the team to test, refine and develop cutting edge techniques to support higher quality outputs and analytics from MS instruments. Andrew is also the Lab Head of the Walter and Eliza Hall Institute of Medical Research’s Proteomics Research Laboratory.