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Literature summary for 2.3.1.48 extracted from

  • Ouyang, C.; Mu, J.; Lu, Q.; Li, J.; Zhu, H.; Wang, Q.; Zou, M.H.; Xie, Z.
    Autophagic degradation of KAT2A/GCN5 promotes directional migration of vascular smooth muscle cells by reducing TUBA/alpha-tubulin acetylation (2019), Autophagy, 2019, 1-18 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene KAT2A, recombinant expression in HeLa cells, overexpressed Flag-KAT2A does not associate with SQSTM1 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
autophagosome
-
Homo sapiens 5776
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-
mitoplast the Gcn5 protein is present inside mitoplasts Saccharomyces cerevisiae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine Saccharomyces cerevisiae
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Saccharomyces cerevisiae D273-10B/A1
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Saccharomyces cerevisiae W303-1A
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40 Homo sapiens
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
?
acetyl-CoA + [protein]-L-lysine Saccharomyces cerevisiae
-
CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine Homo sapiens
-
CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine Saccharomyces cerevisiae D273-10B/A1
-
CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine Saccharomyces cerevisiae W303-1A
-
CoA + [protein]-N6-acetyl-L-lysine
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92830
-
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae D273-10B/A1
-
-
-
Saccharomyces cerevisiae W303-1A
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the histone acetyltransferase KAT2A/GCN5 binds directly to the autophagosome protein MAP1LC3/LC3 (microtubule associated protein 1 light chain) via a conserved LC3-interacting region (LIR) domain. This interaction is required for KAT2A sequestration in autophagosomes and degradation by lysosomal acid hydrolases. Suppression of autophagy results in KAT2A accumulation. The LIR domain of KAT2A is required for KAT2A degradation Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
aortic smooth muscle cell
-
Homo sapiens
-
HeLa cell
-
Homo sapiens
-
smooth muscle cell
-
Saccharomyces cerevisiae
-
smooth muscle cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Saccharomyces cerevisiae CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Saccharomyces cerevisiae D273-10B/A1 CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Saccharomyces cerevisiae W303-1A CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
-
Homo sapiens CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40 KAT2A acetylates Lys40 of TUBA Homo sapiens CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
?
acetyl-CoA + [protein]-L-lysine
-
Saccharomyces cerevisiae CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Homo sapiens CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Saccharomyces cerevisiae D273-10B/A1 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Saccharomyces cerevisiae W303-1A CoA + [protein]-N6-acetyl-L-lysine
-
?

Synonyms

Synonyms Comment Organism
Gcn5
-
Saccharomyces cerevisiae
Gcn5
-
Homo sapiens
histone acetyltransferase
-
Homo sapiens
KAT2
-
Saccharomyces cerevisiae
Kat2A
-
Homo sapiens
KAT2A/GCN5
-
Homo sapiens
lysine acetyltransferase 2
-
Homo sapiens
lysine-acetyltransferase
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Saccharomyces cerevisiae
acetyl-CoA
-
Homo sapiens

General Information

General Information Comment Organism
malfunction GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions Saccharomyces cerevisiae
metabolism in HeLa cells, ectopically overexpressed recombinant MYC-LC3 associates with endogenous KAT2A, but overexpressed Flag-KAT2A does not associate with SQSTM1. Gene silencing of SQSTM1 does not disrupt the association between KAT2A and LC3 in HeLa cells, suggesting that KAT2A physically interacts with LC3, and SQSTM1 is not involved in the interaction between KAT2A and LC3 Homo sapiens
physiological function in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview Saccharomyces cerevisiae
physiological function the histone acetyltransferase KAT2A/GCN5 (lysine acetyltransferase 2) acetylates TUBA in vascular smooth muscle cells leading to microtubule instability and promotion of VSMC migration. Deacetylation of TUBA and perturbation of microtubule stability via selective autophagic degradation of KAT2A are essential for autophagy-promoting VSMC migration Homo sapiens