Journal article

The SOCS box domain of SOCS3: Structure and interaction with the elonginBC-cullin5 ubiquitin ligase

Jeffrey J Babon, Jennifer K Sabo, Alfreda Soetopo, Shenggen Yao, Michael F Bailey, Jian-Guo Zhang, Nicos A Nicola, Raymond S Norton

JOURNAL OF MOLECULAR BIOLOGY | ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD | Published : 2008

Abstract

Suppressor of cytokine signalling 3 (SOCS3) is responsible for regulating the cellular response to a variety of cytokines, including interleukin 6 and leukaemia inhibitory factor. Identification of the SOCS box domain led to the hypothesis that SOCS3 can associate with functional E3 ubiquitin ligases and thereby induce the degradation of bound signalling proteins. This model relies upon an interaction between the SOCS box, elonginBC and a cullin protein that forms the E3 ligase scaffold. We have investigated this interaction in vitro using purified components and show that SOCS3 binds to elonginBC and cullin5 with high affinity. The SOCS3-elonginBC interaction was further characterised by de..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council (NHMRC), Australia


Awarded by National Institutes of Health (Bethesda, MID)


Awarded by NATIONAL CANCER INSTITUTE


Funding Acknowledgements

We thank Tracy Willson for the gift of plasmids. This work was supported in part by the National Health and Medical Research Council (NHMRC), Australia (program grant 257500 and project grant 461260) and the National Institutes of Health (Bethesda, MID) grant CA22556. R.S.N. and N.A.N acknowledge fellowship support from the NHMRC.