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Literature summary for 2.3.1.108 extracted from

  • Wong, V.; Picci, C.; Swift, M.; Levinson, M.; Willis, D.; Langley, B.
    alpha-Tubulin acetyltransferase s a novel target mediating neurite growth inhibitory effects of chondroitin sulfate proteoglycans and myelin-associated glycoprotein (2018), eNeuro, 5, e0240 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Mus musculus Q8K341
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-

Source Tissue

Source Tissue Comment Organism Textmining
neuron primary mouse cortical neuron Mus musculus
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Synonyms

Synonyms Comment Organism
ATAT1
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Mus musculus

General Information

General Information Comment Organism
physiological function exposure of primary mouse cortical neurons to soluble chondroitin sulfate proteoglycans and myelin-associated glycoprotein substrates causes an acute and RhoA-kinase-dependent reduction in alpha-tubulin acetylation and Atat1 protein levels, without changes to either axonal histone deacetylase-6 levels or histonedeacetylase-6 activity. The chondroitin sulfate proteoglycans and myelin-associated glycoprotein-induced reduction in Atat1 occurs primarily in the distal and middle regions of neurites and reconstitution of Atat1, either by Rho-associated kinase inhibition or lentiviral-mediated Atat1 overexpression, can restore neurite growth. Chondroitin sulfate proteoglycans and myelin-associated glycoprotein signaling decreases Atat1 levels posttranscriptionally via a Rho-associated kinase-dependent increase in Atat1 protein turnover Mus musculus