The P151L mutation in the B-box1 domain of MID1 causes midline defects in X-linked Opitz G Syndrome. MID1 is known to be a key regulator of phosphatase PP2A through formation of a complex with its catalytic (PP2Ac) and regulatory (α4) subunits. Wright et al. show that this mutation retains B-box1 domain structure and E3 ligase activity (star) but blocks interaction with α4, indicating disruption of the MID1-α4-PP2Ac complex.
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http://dx.doi.org/10.1111/febs.14149 | DOI Listing |
Cell Discov
November 2024
Shanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, School of Medicine and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Int J Biol Macromol
January 2024
State Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China. Electronic address:
Structure
September 2023
Department of Molecular Biology and Biophysics, UCONN Health, Farmington, CT 06032, USA. Electronic address:
Biochemistry
March 2023
Department of Chemistry, George Washington University, 800 22nd St NW, Washington, D.C. 20052, United States.
The MID1 TRIM protein is important for ventral midline development in vertebrates, and mutations of its B-box1 domain result in several birth defects. The B-box1 domain of the human MID1 protein binds two zinc atoms and adopt a similar ββα-RING structure. This domain is required for the efficient ubiquitination of protein phosphatase 2A, alpha4, and fused kinase.
View Article and Find Full Text PDFBiophys Chem
August 2022
Department of Molecular Biology and Biophysics, UCONN Health, Farmington, CT 06032, USA. Electronic address:
The small, ubiquitin-like modifier SUMO is covalently attached to substrates by the enzyme UBC9. SUMO conjugation of substrates often requires an E3 ligase, which ensures substrate specificity by simultaneously binding UBC9 and the substrate. E3 SUMO ligases commonly use a RING domain to engage UBC9.
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