Literature summary for 2.3.1.6 extracted from

Morey, T.; Winick-Ng, W.; Seah, C.; Jane Rylett, R.
Chaperone-mediated regulation of choline acetyltransferase protein stability and activity by HSC/HSP70, HSP90, and p97/VCP (2017), Front. Mol. Neurosci., 10, 415 .

Search for more literature for 2.3.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293 cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A513T	mutant associated with congenital myasthenic syndrome, shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition	Homo sapiens
P17A/P19A	mutant shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition	Homo sapiens
V18M	mutant associated with congenital myasthenic syndrome, shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P28329	-	-

Synonyms

Synonyms	Comment	Organism
ChAT	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	enzyme interacts with heat shock proteins HSC/HSP70 and HSP90. Inhibition of heat shock proteins reduces cellular ChAT activity and solubility, and enhances the ubiquitination and proteasome-dependent loss of ChAT protein. The effects of HSP inhibition are greater for mutant ChAT proteins P17A/P19A and congenital myasthenic syndrome-related mutants V18M and A513T compared to wild-type ChAT. siRNA-mediated knock-down of E3 ubiquitin ligase CHIP has no effect on either wild-type or mutant ChAT protein levels. Inhibition of the endoplasmic reticulum and heat shock protein-associated cochaperone p97/VCP prevents degradation of ubiquitinated ChAT	Homo sapiens

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Release 2023.1 (January 2023)