Premium
Mechanism of midline defect‐causing mutation P151L in MID 1 revealed
Author(s) -
Nicholson Linda K.
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14149
Subject(s) - mutation , protein phosphatase 2 , ubiquitin ligase , regulator , protein subunit , phosphatase , domain (mathematical analysis) , dna ligase , biology , genetics , chemistry , microbiology and biotechnology , ubiquitin , dna , phosphorylation , gene , mathematical analysis , mathematics
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.