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Article

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.

Proceedings of the National Academy of Sciences of the United States of America - 5 Jun 2001

Liu J, Prickett T D, Elliott E, Meroni G, Brautigan D L

Abstract excerpt

Opitz syndrome (OS) is a human genetic disease characterized by deformities such as cleft palate that are attributable to defects in embryonic development at the midline. Gene mapping has identified OS mutations within a protein called Mid1. Wild-type Mid1 predominantly colocalizes with microtubules, in contrast to mutant versions of Mid1 that appear clustered in the cytosol. Using yeast two-hybrid screening, we...

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Identifiers

PMID: 11371618
DOI: 10.1073/pnas.111154698
PMCID: PMC34408

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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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.PMID 11371618Read ↗

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

The Opitz syndrome gene product, MID1, associates with microtubules.Semantic proximity Read ↗

Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A.Semantic proximity Read ↗

Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle.Semantic proximity Read ↗

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The MID1/PP2A complex: a key to the pathogenesis of Opitz BBB/G syndrome.Semantic proximity Read ↗

The MID1 gene product in physiology and disease.Semantic proximity Read ↗

MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disordersSemantic proximity Read ↗

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

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