1. Ozz Molecular Cell Volume 13, Issue 4, Pages 451-453 (February 2004)
Geng Wu, Chunming Liu, Xi He 
Molecular Cell 
Volume 13, Issue 4, Pages (February 2004)
DOI: /S (04)

2. Figure 1
Distinct E3 Ubiquitin Ligase Complexes for β-Catenin (Cadherin) and Cadherin/β-Catenin Function in Sarcomere Organization
(A) The SCFβ-TrCP E3 complex (left) and the Ebi-E3 complex (right) for cytosolic β-catenin. β-Trcp recognizes amino-terminally phosphorylated β-catenin, whose phosphorylation is inhibited by Wnt. Ebi binds to the β-catenin amino-terminal region in a phosphorylation-independent manner. Siah-1 expression is induced by p53.
(B) The Ozz-E3 complex (left) and Hakai E3 (right) for membrane-bound β-catenin. Ozz binds to the carboxyl region of β-catenin. Hakai binds to tyrosine-phosphorylated E-cadherin and ubiquitinates both E-cadherin and β-catenin for endocytosis and lysosomal degradation or recycling.
(C) The cadherin/β-catenin complex may function to tether and align sarcomeres within and between myofibers (muscle cells) via the association with the Z disc of the sarcomere. The integrin and dystroglycan complexes are also involved in the tethering function. ECM, extracellular matrix; Sarcolemma, muscle plasma membrane. Courtesy of T. Nastasi and A. d'Azzo.
Molecular Cell  , DOI: ( /S (04) )