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Article

XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.

PloS one - 1 Jan 2014

Wright Katharine M, Wu Kuanlin, Babatunde Omotolani, Du Haijuan, Massiah Michael A

Abstract excerpt

MID1 catalyzes the ubiquitination of the protein alpha4 and the catalytic subunit of protein phosphatase 2A. Mutations within the MID1 Bbox1 domain are associated with X-linked Opitz G syndrome (XLOS). Our functional assays have shown that mutations of Ala130 to Val or Thr, Cys142 to Ser and Cys145 to Thr completely disrupt the polyubiquitination of alpha4. Using NMR spectroscopy, we characterize the effect of...

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Source

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Identifiers

PMID: 25216264
DOI: 10.1371/journal.pone.0107537
PMCID: PMC4162623

Genes

MID1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.PMID 25216264Read ↗

Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.Semantic proximity Read ↗

Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.Semantic proximity Read ↗

Mechanism of midline defect-causing mutation P151L in MID1 revealed.Semantic proximity Read ↗

New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome.Semantic proximity Read ↗

Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1.Semantic proximity Read ↗

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation.Semantic proximity Read ↗

A structure-function study of MID1 mutations associated with a mild Opitz phenotype.Semantic proximity Read ↗

X-linked Opitz syndrome: novel mutations in the MID1 gene and redefinition of the clinical spectrum.Semantic proximity Read ↗

DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding.Semantic proximity Read ↗

Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the carboxy-terminal domain.Semantic proximity Read ↗

Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.Semantic proximity Read ↗

Nox4 B-loop creates an interface between the transmembrane and dehydrogenase domains.Semantic proximity Read ↗

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