Phosphorylation Modulates Aspartyl-(Asparaginyl)-β Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells.

ABSTRACT:

Background

Abundant aspartyl-asparaginyl-β-hydroxylase (ASPH) expression supports robust neuronal migration during development, and reduced ASPH expression and function, as occur in fetal alcohol spectrum disorder, impair cerebellar neuron migration. ASPH mediates its effects on cell migration via hydroxylation-dependent activation of Notch signaling networks. Insulin and Insulin-like growth factor (IGF-1) stimulate ASPH mRNA transcription and enhance ASPH protein expression by inhibiting Glycogen Synthase Kinase-3β (GSK-3β). This study examines the role of direct GSK-3β phosphorylation as a modulator of ASPH protein expression and function in human cerebellar-derived PNET2 cells.

Methods

Predicted phosphorylation sites encoded by human ASPH were ablated by S/T→A site-direct

SUBMITTER: Tong M 

PROVIDER: S-EPMC5878085 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature