Summary of known FAT substratesa
FAT substrate | Known function in vivo | Known FAT enzyme in vitro | Functional effect of acetylation | Observed or predicted effect on transcription |
---|---|---|---|---|
Nonhistone chromatin proteins | ||||
HMG1 | Chromatin component | p300/CBP | ND | ND |
HMG2 | Chromatin component | ND | ND | ND |
Yeast Sin1 | Transcriptional regulator | Likely Gcn5 | ND | ND |
HMG14 | Nucleosome binding | p300/CBP | Nucleosome binding weakened | ND |
HMG17 | Nucleosome binding | PCAF | Nucleosome binding weakened | ND |
HMG I(Y) | Enhanceosome component | PCAF | Enhanceosome assemblyb | Positiveb |
p300/CBP | Enhanceosome disruption | Negative | ||
Transcriptional activators | ||||
p53 | Tumor suppressor | PCAF, p300/CBP | Increased DNA binding | Positive |
c-Myb | Cell proliferation, differentiation | p300/CBP, GCN5 | Increased DNA binding | Positive |
GATA-1 | Blood cell differentiation | p300/CBP | DNA binding may be affected | Positive |
EKLF | Globin gene expression | p300/CBP | Inhibitory domain modified | Positive |
MyoD | Muscle differentiation | PCAF | Increased DNA binding | Positive |
E2F | Cell cycle control | PCAF | Increased DNA binding | Positive |
dTCF | Developmental regulation | p300/CBP | Coactivator interaction disrupted | Negative |
HIV Tat | HIV-1 transactivation | PCAF | Increased CDK9 binding | Positive |
p300/CBP | Release from TAR RNA | Positive | ||
Nuclear receptor coactivators | Transcriptional response to hormone signals | |||
ACTR | p300/CBP | Receptor interaction disrupted | Negative | |
SRC-1 | p300/CBP | ND | ND | |
TIF2 | p300/CBP | ND | ND | |
General transcription factors | General transcriptional machinery components | |||
TFIIE | PCAF, p300/CBP, TAFII250 | ND | ND | |
TFIIF | PCAF, p300/CBP | ND | ND | |
Importin-α7, Rch1 | Nuclear import | p300/CBP | Increased importin-β binding | ND (may be unrelated to transcription) |
α-Tubulin | Microtubule component | ND | ND; stabilized microtubules become acetylated | ND (may be unrelated to transcription) |
↵a The FAT substrates characterized in vitro were human, mouse, or rat versions with the exception of yeast Sin1 and Drosophila TCF. The other substrates (HMG2 and α-tubulin) have unknown FAT enzymes but were observed to contain one or more acetylated internal lysines in various cell extracts. ND, not determined.
↵b D. Thanos, personal communication.