COMMD Proteins and the Control of the NFκB Pathway

Gabriel N. Maine and Ezra Burstein

volume 6 | issue 6

15 March 2007
Pages: 672 - 676

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The COMM domain containing (COMMD) family of proteins represents a recently discovered set of evolutionarily conserved factors characterized by the presence of a defining carboxy-terminal motif. In vertebrates, there are ten members of the family, and among their emerging functions the control of the transcription factor NF-κB has been most extensively studied. NFκB plays a critical role in a number of homeostatic processes in multicellular organisms, including the regulation of immunity and cell survival. COMMD proteins inhibit NF-κB mediated gene expression, and recent mechanistic studies have revealed that COMMD1 controls the ubiquitination of NFκB subunits, an event linked to transcriptional termination. COMMD1 binds to a multimeric ubiquitin ligase containing Elongins B/C, Cul2 and SOCS1 (ECSSOCS1). In this complex, COMMD1 facilitates the binding of NFκB subunits to the ligase, thereby promoting their ubiquitination and degradation. Additional insights gained from these studies indicate that COMMD proteins likely play a broader role in cellular homeostasis through their participation in the ubiquitination pathway.

Authors

Gabriel N. Maine

University of Michigan Medical School, Ann Arbor, Michigan

Ezra Burstein

University of Michigan Medical School, Ann Arbor, Michigan

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: