Pub. Date : 2014 Aug 1
PMID : 24962578
16 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Tyr-94 phosphorylation inhibits pyruvate dehydrogenase phosphatase 1 and promotes tumor growth. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 2 | We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 3 | We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 4 | We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 5 | We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 6 | In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 7 | In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 8 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 9 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 10 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 11 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 12 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 13 | Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 14 | We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 15 | We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |
| 16 | Together, our findings suggest that phosphorylation at different tyrosine residues inhibits PDP1 through independent mechanisms, which act in concert to regulate PDC activity and promote the Warburg effect. | Tyrosine | pyruvate dehydrogenase phosphatase catalytic subunit 1 | Homo sapiens |