LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation

• Published in: The EMBO journal Vol. 21; no. 1-2; pp. 93 - 102
• Main Authors: Nie, Jing, McGill, Melanie A., Dermer, Matt, Dho, Sascha E., Wolting, Cheryl D., McGlade, C. Jane
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 15.01.2002; Blackwell Publishing Ltd; Oxford University Press
• Subjects: Animals; Binding Sites; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell Line; CHO Cells; Cricetinae; Dogs; Humans; Ligases - genetics; Ligases - metabolism; LNX; Membrane Proteins - genetics; Membrane Proteins - metabolism; Mice; Mutagenesis, Site-Directed; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Numb; PDZ domain; Protein Structure, Tertiary; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; RING finger; Substrate Specificity; Ubiquitin - metabolism; ubiquitin ligase; Ubiquitin-Protein Ligases

LNX is a RING finger and PDZ domain containing protein that interacts with the cell fate determinant Numb. To investigate the function of LNX, we tested its RING finger domain for ubiquitin ligase activity. The isolated RING finger domain was able to function as an E2‐dependent, E3 ubiquitin ligase...