Reactome | PRKACA phosphorylates TFAM in the mitochondrial matrix

PRKACA phosphorylates TFAM in the mitochondrial matrix

Stable Identifier

R-HSA-9838321

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial matrix

ReviewStatus

5/5

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PRKACA phosphorylates TFAM in the mitochondrial matrix

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In the mitochondrial matrix, cAMP-dependent kinase PKA alpha (PRKACA) phosphorylates the HMG domains of the mitochondrial transcription factor TFAM (Lu et al. 2013). Phosphorylation prevents TFAM from binding DNA and causes degradation of TFAM by the LONP1 protease, which only degrades TFAM that is not bound to DNA (Lu et al. 2013). Phosphorylation of serine residues 55, 56, and 61 in the HMG1 domain but not serine residue 160 in the HMG2 domain are required for degradation by LONP1 (Lu et al. 2013).

Literature References

PubMed ID	Title	Journal	Year
23201127	Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease Lu, B, Lee, J, Nie, X, Li, M, Morozov, YI, Venkatesh, S, Bogenhagen, DF, Temiakov, D, Suzuki, CK	Mol Cell	2013