PRKACA phosphorylates TFAM in the mitochondrial matrix

Stable Identifier
R-HSA-9838321
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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

Temiakov, D, Bogenhagen, DF, Li, M, Nie, X, Venkatesh, S, Morozov, YI, Suzuki, CK, Lee, J, Lu, B

Mol Cell 2013
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Catalyst Activity

cAMP-dependent protein kinase activity of PRKACA [mitochondrial matrix]

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