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N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Samuel Zolg1, Laura Donzelli1, Ruth Geiss-Friedlander1
1Institute of Molecular Medicine and Cell Research, Faculty of Medicine, University of Freiburg, Stefan-Meier-Str. 17, 79104, Freiburg, Germany.
Dipeptidyl peptidase 9 (DPP9) regulates key proteins like BRCA2, impacting DNA repair and cancer. This review explores DPP9
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Dipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase.
- DPP9 has physiological roles in immunity, DNA repair, and mitochondrial homeostasis.
- DPP9 deregulation is associated with cancer progression and immune defects.
Purpose of the Study:
- To review key concepts of protein processing by DPP9.
- To discuss DPP9's role in the N-degron pathway.
- To explore non-enzymatic functions and regulation of DPP9.
Main Methods:
- Review of existing literature on Dipeptidyl peptidase 9 (DPP9).
- Analysis of DPP9's substrate processing mechanisms.
- Examination of DPP9's interactome and regulatory partners.
Main Results:
- DPP9 uniquely cleaves peptide bonds after proline, acting as a molecular switch.
- DPP9 regulates critical proteins, including the tumor suppressor BRCA2.
- DPP9's interactome includes SUMO1, Filamin A, NLRP1, and CARD8, influencing its regulation and function.
Conclusions:
- DPP9 is a crucial regulator of protein homeostasis with implications in cancer and immunity.
- Understanding DPP9's enzymatic and non-enzymatic roles is vital for therapeutic development.
- Further research into DPP9's interactome will elucidate its complex regulatory network.
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