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TitlePolyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.
Journal, issue, pagesSci Rep, Vol. 14, Issue 1, Page 9923, Year 2024
Publish dateApr 30, 2024
AuthorsNina Kunová / Gabriela Ondrovičová / Jacob A Bauer / Veronika Krajčovičová / Matyáš Pinkas / Barbora Stojkovičová / Henrieta Havalová / Veronika Lukáčová / Lenka Kohútová / Július Košťan / Lucia Martináková / Peter Baráth / Jiří Nováček / Sebastian Zoll / Sami Kereϊche / Eva Kutejová / Vladimír Pevala /
PubMed AbstractPhosphorylation plays a crucial role in the regulation of many fundamental cellular processes. Phosphorylation levels are increased in many cancer cells where they may promote changes in ...Phosphorylation plays a crucial role in the regulation of many fundamental cellular processes. Phosphorylation levels are increased in many cancer cells where they may promote changes in mitochondrial homeostasis. Proteomic studies on various types of cancer identified 17 phosphorylation sites within the human ATP-dependent protease Lon, which degrades misfolded, unassembled and oxidatively damaged proteins in mitochondria. Most of these sites were found in Lon's N-terminal (NTD) and ATPase domains, though little is known about the effects on their function. By combining the biochemical and cryo-electron microscopy studies, we show the effect of Tyr186 and Tyr394 phosphorylations in Lon's NTD, which greatly reduce all Lon activities without affecting its ability to bind substrates or perturbing its tertiary structure. A substantial reduction in Lon's activities is also observed in the presence of polyphosphate, whose amount significantly increases in cancer cells. Our study thus provides an insight into the possible fine-tuning of Lon activities in human diseases, which highlights Lon's importance in maintaining proteostasis in mitochondria.
External linksSci Rep / PubMed:38688959 / PubMed Central
MethodsEM (single particle)
Resolution2.88 - 8.47 Å
Structure data

16915

8ojl

EMDB-16915, PDB-8ojl:
Human Mitochondrial Lon Y394E Mutant ADP Bound
Method: EM (single particle) / Resolution: 2.88 Å

16923

8oka

EMDB-16923, PDB-8oka:
Human Mitochondrial Lon Y394F Mutant ADP Bound
Method: EM (single particle) / Resolution: 3.89 Å

16970

8om7

EMDB-16970, PDB-8om7:
Human Mitochondrial Lon Y186E Mutant ADP Bound
Method: EM (single particle) / Resolution: 3.74 Å

17213

8ovf

EMDB-17213, PDB-8ovf:
Human Mitochondrial Lon Y186F Mutant ADP Bound
Method: EM (single particle) / Resolution: 7.23 Å

17214

8ovg

EMDB-17214, PDB-8ovg:
Human Mitochondrial Lon Y186E Mutant ADP Bound
Method: EM (single particle) / Resolution: 8.47 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Human mitochondrial AAA+ protease / motor protein

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