| + |
PRKCE | up-regulates activity 
phosphorylation
|
ALDH2 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271864 |
Ser296 |
KSPNIIMsDADMDWA |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271865 |
Thr202 |
KLGPALAtGNVVVMK |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271866 |
Thr429 |
MQILKFKtIEEVVGR |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
AMPK | up-regulates activity
phosphorylation
|
ALDH2 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271862 |
Thr356 |
GNPFDSKtEQGPQVD |
Mus musculus |
Macrophage |
| pmid |
sentence |
| 30375985 |
Further studies demonstrate that in the absence of LDLR, AMPK phosphorylates ALDH2 at threonine 356 and enables its nuclear translocation. Nuclear ALDH2 interacts with HDAC3 and represses transcription of a lysosomal proton pump protein ATP6V0E2, critical for maintaining lysosomal function, autophagy, and degradation of oxidized low-density lipid protein. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
ALDH2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271863 |
Thr356 |
GNPFDSKtEQGPQVD |
Mus musculus |
Macrophage |
| pmid |
sentence |
| 30375985 |
Further studies demonstrate that in the absence of LDLR, AMPK phosphorylates ALDH2 at threonine 356 and enables its nuclear translocation. Nuclear ALDH2 interacts with HDAC3 and represses transcription of a lysosomal proton pump protein ATP6V0E2, critical for maintaining lysosomal function, autophagy, and degradation of oxidized low-density lipid protein. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ALDH2 | up-regulates activity
binding
|
HDAC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271867 |
|
|
in vitro |
|
| pmid |
sentence |
| 28056995 |
Consistent with previous data, HDAC3 only bound to the ATP6V0E2 promoter in the presence of ALDH2.|Taken together, our data demonstrate that in the macrophages of LDLR-KO or ALDH2 rs671 mutant, AMPK phosphorylates ALDH2 at T356, which enables its nuclear translocation. Once in the nucleus, ALDH2 binds to HDAC3 and suppresses the transcription and protein expression of ATP6V0E2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
ALDH2
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