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Article

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

PloS one - 1 Jan 2008

Aranda-Orgillés Beatriz, Aigner Johanna, Kunath Melanie, Lurz Rudi, Schneider Rainer, Schweiger Susann

Abstract excerpt

Mutations in the MID1 protein have been found in patients with Opitz BBB/G syndrome (OS), which is characterised by multiple malformations of the ventral midline. MID1 is a microtubule-associated protein that stabilizes microtubules and, in association with the regulatory subunit of protein phosphatase 2A (PP2A), alpha4, provides ubiquitin ligase activity for the ubiquitin-specific modification of PP2A. Using...

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Identifiers

PMID: 18949047
DOI: 10.1371/journal.pone.0003507
PMCID: PMC2568803

Genes

MID1

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Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A.PMID 18949047Read ↗

The MID1 protein is a central player during development and in disease.Semantic proximity Read ↗

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

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

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

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

The MID1 gene product in physiology and disease.Semantic 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 ↗

aura/mid1ip1Lregulates the cytoskeleton at the zebrafish egg-to-embryo transitionSemantic proximity Read ↗

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

Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22.Semantic proximity Read ↗

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