lissencephaly/phosphatase

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AiltTrialacha cliniciúlaPaitinní

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[Molecular mechanism of lissencephaly--how LIS1 and NDEL1 regulate cytoplasmic dynein?].

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Logáil Isteach / Cláraigh

Lissencephaly is a devastating neurological disorder characterized by smooth cerebral surface, thick cortex and dilated lateral ventricules due to defective neuronal migration. Lis1 was identified as a mutated gene in classical lissencephaly patients, and turned out to be a beta-subunit of platelet

Lissencephaly and LIS1: insights into the molecular mechanisms of neuronal migration and development.

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Logáil Isteach / Cláraigh

Lissencephaly is a severe human neuronal migration defect characterized by a smooth cerebral surface, mental retardation and seizures. LIS1 was first gene cloned in an organism important for neuronal migration, as it was deleted or mutated in patients with lissencephaly in a heterozygous fashion.

Doublecortin microtubule affinity is regulated by a balance of kinase and phosphatase activity at the leading edge of migrating neurons.

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Logáil Isteach / Cláraigh

Doublecortin (Dcx) is a microtubule-associated protein that is mutated in X-linked lissencephaly (X-LIS), a neuronal migration disorder associated with epilepsy and mental retardation. Although Dcx can bind ubiquitously to microtubules in nonneuronal cells, Dcx is highly enriched in the leading

Site-specific dephosphorylation of doublecortin (DCX) by protein phosphatase 1 (PP1).

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Logáil Isteach / Cláraigh

Mutations in doublecortin (DCX) cause X-linked lissencephaly ("smooth brain") and double cortex syndrome in humans. DCX is highly phosphorylated in migrating neurons. Here, we demonstrate that dephosphorylation of specific sites phosphorylated by JNK is mediated by Neurabin II, which recruits the

Inhibition of PP2A by LIS1 increases HIV-1 gene expression.

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Logáil Isteach / Cláraigh

BACKGROUND Lissencephaly is a severe brain malformation in part caused by mutations in the LIS1 gene. LIS1 interacts with microtubule-associated proteins, and enhances transport of microtubule fragments. Previously we showed that LIS1 interacts with HIV-1 Tat protein and that this interaction was

LIS1 is a microtubule-associated phosphoprotein.

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Logáil Isteach / Cláraigh

Lissencephaly, a severe brain malformation, may be caused by mutations in the LIS1 gene. LIS1 encodes a microtubule-associated protein (MAP) that is also part of the enzyme complex, platelet-activating factor acetylhydrolase. LIS1 is also found in a complex with two protein kinases; a T-cell

New syndrome of simplified gyral pattern, micromelia, dysmorphic features and early death.

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Logáil Isteach / Cláraigh

We report two sisters with a new syndrome of simplified gyral pattern, normal head circumference at birth but with subsequent development of microcephaly, intractable seizures, and early death. Dysmorphic features included coarse face, hypertrichosis, short nose, paranasal widening, long philtrum,

Multisite phosphorylation of doublecortin by cyclin-dependent kinase 5.

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Logáil Isteach / Cláraigh

Doublecortin (DCX) is a 40 kDa microtubule-associated protein required for normal neural migration and cortical layering during development. Mutations in the human DCX gene cause a disruption of cortical neuronal migration. Defects in cdk5 (cyclin-dependent kinase 5) also cause defects in neural

Different Doublecortin (DCX) Patient Alleles Show Distinct Phenotypes in Cultured Neurons: EVIDENCE FOR DIVERGENT LOSS-OF-FUNCTION AND "OFF-PATHWAY" CELLULAR MECHANISMS.

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Logáil Isteach / Cláraigh

Doublecortin on the X-chromosome (DCX) is a neuronal microtubule-binding protein with a multitude of roles in neurodevelopment. In humans, DCX is a major genetic locus for X-linked lissencephaly. The best studied defects are in neuronal migration during corticogenesis and in the hippocampus, as well

Neurabin II mediates doublecortin-dephosphorylation on actin filaments.

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Logáil Isteach / Cláraigh

Mutations in the human Doublecortin (DCX) gene cause X-linked lissencephaly, a neuronal migration disorder. DCX binds to microtubules and actin filaments. Association of Dcx with F-actin is regulated by site-specific phosphorylation and by neurabin II, an F-actin binding protein that also binds to

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