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Literature summary for 2.3.2.8 extracted from

  • Wang, J.; Han, X.; Leu, N.A.; Sterling, S.; Kurosaka, S.; Fina, M.; Lee, V.M.; Dong, D.W.; Yates, J.R.; Kashina, A.
    Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration (2017), Sci. Rep., 7, 11323 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.8

Protein Variants

Protein Variants Comment Organism
additional information generation of Ate1 knockout mice and Ate1 knockout mouse embryonic fibroblasts, phenotypes, overview. alpha-Syn-transfected Ate1 knockout cells are treated with chloroquine and bafilomycin, the inhibitors of lysosomal degradation and autophagy previously shown to interfere with alpha-syn removal from normal cells. Neither of these treatments in Ate1 knockout leads to the expected increase in intracellular levels of alpha-syn, suggesting that neither lysosomal degradation nor autophagy contribute substantially to the removal of alpha-syn, in the absence of arginylation Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginyl-tRNAArg + alpha-synuclein Mus musculus alpha-syn is arginylated in vitro and in vivo tRNAArg + L-arginyl-[alpha-synuclein]
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 ?
L-arginyl-tRNAArg + protein Mus musculus
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 tRNAArg + L-arginyl-[protein]
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9Z2A5
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-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
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hippocampus
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 Mus musculus
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neuron
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 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginyl-tRNAArg + alpha-synuclein alpha-syn is arginylated in vitro and in vivo Mus musculus tRNAArg + L-arginyl-[alpha-synuclein]
-
 ?
L-arginyl-tRNAArg + protein
-
 Mus musculus tRNAArg + L-arginyl-[protein]
-
 ?

Synonyms

Synonyms Comment Organism
Ate1
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 Mus musculus

General Information

General Information Comment Organism
malfunction deletion of Ate1 in mice leads to embryonic lethality and impairments in multiple physiological systems, including cardiovascular development, angiogenesis, muscle contraction, and cell migration. Lack of arginylation leads to increased Alpha synuclein (alpha-syn) aggregation and causes the formation of larger pathological aggregates in neurons, accompanied by impairments in its ability to be cleared via normal degradation pathways. In the mouse brain, lack of arginylation leads to an increase in alpha-syn's insoluble fraction, accompanied by behavioral changes characteristic for neurodegenerative pathology. Lack of arginylation in the brain leads to neurodegeneration Mus musculus
physiological function protein arginylation is a posttranlsational modification mediated by arginyltransferase ATE1 that transfers Arg from tRNA directly to protein targets. Protein arginylation targets alpha-synuclein, facilitates normal brain health, and prevents neurodegeneration. Alpha-synuclein (alpha-syn) is a central player in neurodegeneration. It is a highly efficient substrate for arginyltransferase ATE1 and is arginylated in vivo by a mid-chain mechanism that targets the acidic side chains of E46 and E83. alpha-Syn arginylation can be a factor that facilitates normal alpha-syn folding and function in vivo. Arginylation reduces aggregation of pre-formed alpha-syn fibrils and partially prevents alpha-syn-induced seeding of pathological aggregates in cultured neurons, overview Mus musculus