Abstract
The inducible and reversible modification of proteins with polyubiquitin chains has emerged as one of the most common and versatile means of protein modification. Ubiquitin contains 7 lysine residues, each of which can serve as an acceptor site for formation of polyubiquitin chains. In addition, the C-terminal glycine of one ubiquitin molecule can form a conventional peptide bond with the N-terminal methionine of an acceptor ubiquitin, leading to the formation of linear polyubiquitin chains. Linear ubiquitin chains stabilize proteins and play critical roles in signaling complex assembly. The linear ubiquitin chain assembly complex (LUBAC) consists of at least 3 proteins: HOIP (also known as RNF31), HOIL-1L (also known as RBCK1), and SHARPIN [1-6].
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