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Chemical Blockage of the Mitochondrial Rhomboid Protease PARL by Novel Ketoamide Inhibitors Reveals Its Role in PINK1/Parkin-Dependent Mitophagy

https://doi.org/10.1021/acs.jmedchem.2c01092

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Solubilization of Membrane Proteins into Functional Lipid‐Bilayer Nanodiscs Using a Diisobutylene/Maleic Acid Copolymer

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Interrogating Membrane Protein Conformational Dynamics within Native Lipid Compositions

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Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control

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The p.S77N presenilin‐associated rhomboid‐like protein mutation is not a frequent cause of early‐onset Parkinson's disease

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Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels

inferredcites →https://doi.org/10.1007/s00018-019-03203-4openalex-snapshot

Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond

inferredcites →https://doi.org/10.1016/b978-0-12-385120-8.00015-2openalex-snapshot

Enzymatic Assembly of Overlapping DNA Fragments

inferredcites →https://doi.org/10.1016/j.bbamcr.2017.04.016openalex-snapshot

Rhomboid proteases in human disease: Mechanisms and future prospects

inferredcites →https://doi.org/10.1016/j.cell.2013.10.053openalex-snapshot

Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity

inferredcites →https://doi.org/10.1016/j.celrep.2017.01.029openalex-snapshot

The Mitochondrial Rhomboid Protease PARL Is Regulated by PDK2 to Integrate Mitochondrial Quality Control and Metabolism

inferredcites →https://doi.org/10.1016/j.chembiol.2017.09.007openalex-snapshot

General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases

inferredcites →https://doi.org/10.1016/j.chembiol.2020.08.011openalex-snapshot

Designed Parasite-Selective Rhomboid Inhibitors Block Invasion and Clear Blood-Stage Malaria

inferredcites →https://doi.org/10.1016/j.cub.2011.11.057openalex-snapshot

A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes

inferredcites →https://doi.org/10.1016/j.jbc.2021.100383openalex-snapshot

Insights into the catalytic properties of the mitochondrial rhomboid protease PARL

inferredcites →https://doi.org/10.1016/j.molcel.2015.12.022openalex-snapshot

Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis

inferredcites →https://doi.org/10.1016/j.molcel.2019.01.002openalex-snapshot

Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1

inferredcites →https://doi.org/10.1016/j.tibs.2018.06.009openalex-snapshot

The Rhomboid Superfamily: Structural Mechanisms and Chemical Biology Opportunities

inferredcites →https://doi.org/10.1016/j.tibs.2019.05.002openalex-snapshot

Co-Translational Protein Folding in Lipid Membranes

inferredcites →https://doi.org/10.1021/acs.langmuir.7b03742openalex-snapshot

Formation of Lipid-Bilayer Nanodiscs by Diisobutylene/Maleic Acid (DIBMA) Copolymer

inferredcites →https://doi.org/10.1021/jacs.8b08441openalex-snapshot

Stable and Functional Rhomboid Proteases in Lipid Nanodiscs by Using Diisobutylene/Maleic Acid Copolymers

inferredcites →https://doi.org/10.1021/jo00088a027openalex-snapshot

Coupling N-Methylated Amino Acids Using PyBroP and PyCloP Halogenophosphonium Salts: Mechanism and Fields of Application

inferredcites →https://doi.org/10.1038/embor.2012.14openalex-snapshot

Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment

inferredcites →https://doi.org/10.1038/ncb3488openalex-snapshot

PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis

inferredcites →https://doi.org/10.1038/ncomms9022openalex-snapshot

Rhomboid domain containing 1 promotes colorectal cancer growth through activation of the EGFR signalling pathway

inferredcites →https://doi.org/10.1038/nprot.2006.42openalex-snapshot

The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology

inferredcites →https://doi.org/10.1038/nprot.2007.426openalex-snapshot

Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems

inferredcites →https://doi.org/10.1038/s41598-017-08522-9openalex-snapshot

Structure formation during translocon-unassisted co-translational membrane protein folding

inferredcites →https://doi.org/10.1042/bst20170424openalex-snapshot

Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins

inferredcites →https://doi.org/10.1073/pnas.0408306102openalex-snapshot

Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity

inferredcites →https://doi.org/10.1073/pnas.0604983103openalex-snapshot

Phosphorylation and cleavage of presenilin-associated rhomboid-like protein (PARL) promotes changes in mitochondrial morphology

inferredcites →https://doi.org/10.1073/pnas.0911187107openalex-snapshot

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

inferredcites →https://doi.org/10.1073/pnas.1811938116openalex-snapshot

PARL deficiency in mouse causes Complex III defects, coenzyme Q depletion, and Leigh-like syndrome

inferredcites →https://doi.org/10.1074/jbc.m112.357509openalex-snapshot

Rhomboid Protease PARL Mediates the Mitochondrial Membrane Potential Loss-induced Cleavage of PGAM5

inferredcites →https://doi.org/10.1074/jbc.m116.762849openalex-snapshot

Sensitive Versatile Fluorogenic Transmembrane Peptide Substrates for Rhomboid Intramembrane Proteases

inferredcites →https://doi.org/10.1074/jbc.m313756200openalex-snapshot

Self-regulated Cleavage of the Mitochondrial Intramembrane-cleaving Protease PARL Yields Pβ, a Nuclear-targeted Peptide

inferredcites →https://doi.org/10.1074/mcp.tir118.001099openalex-snapshot

Quantitative Multiplex Substrate Profiling of Peptidases by Mass Spectrometry

inferredcites →https://doi.org/10.1080/15548627.2015.1063763openalex-snapshot

Intramembrane protease PARL defines a negative regulator of PINK1- and PARK2/Parkin-dependent mitophagy

inferredcites →https://doi.org/10.1083/jcb.200910140openalex-snapshot

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

inferredcites →https://doi.org/10.1083/jcb.201008084openalex-snapshot

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

inferredcites →https://doi.org/10.1093/hmg/ddm334openalex-snapshot

Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1

inferredcites →https://doi.org/10.1093/hmg/ddq526openalex-snapshot

PINK1 cleavage at position A103 by the mitochondrial protease PARL

inferredcites →https://doi.org/10.1093/hmg/ddr077openalex-snapshot

Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease

inferredcites →https://doi.org/10.1111/febs.13638openalex-snapshot

Why cells need intramembrane proteases – a mechanistic perspective

inferredcites →https://doi.org/10.1111/j.1471-4159.2011.07253.xopenalex-snapshot

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking

inferredcites →https://doi.org/10.1111/mmi.13021openalex-snapshot

Distinct contribution of T oxoplasma gondii rhomboid proteases 4 and 5 to micronemal protein protease 1 activity during invasion

inferredcites →https://doi.org/10.1128/iai.00011-16openalex-snapshot

Identification and Characterization of a Novel Aspergillus fumigatus Rhomboid Family Putative Protease, RbdA, Involved in Hypoxia Sensing and Virulence

inferredcites →https://doi.org/10.1128/mbio.01795-14openalex-snapshot

Functional Analysis of Rhomboid Proteases during Toxoplasma Invasion

inferredcites →https://doi.org/10.1128/msphere.00035-16openalex-snapshot

RbdB, a Rhomboid Protease Critical for SREBP Activation and Virulence in Aspergillus fumigatus

inferredcites →https://doi.org/10.1135/cccc19950693openalex-snapshot

An Efficient Method for Preparation of Optically Active N-Protected α-Amino Aldehydes from N-Protected α-Amino Alcohols

inferredcites →https://doi.org/10.1152/ajpcell.00589.2019openalex-snapshot

LonP1 regulates mitochondrial network remodeling through the PINK1/Parkin pathway during myoblast differentiation

inferredcites →https://doi.org/10.1177/2472555219857691openalex-snapshot

Structures and Interactions of Transmembrane Targets in Native Nanodiscs

inferredcites →https://doi.org/10.1242/jcs.217745openalex-snapshot

Intramembrane proteolysis at a glance: from signalling to protein degradation

inferredcites →https://doi.org/10.1371/journal.pbio.1000298openalex-snapshot

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

inferredcites →https://doi.org/10.1371/journal.pgen.1004279openalex-snapshot

PINK1-Parkin Pathway Activity Is Regulated by Degradation of PINK1 in the Mitochondrial Matrix

inferredcites →https://doi.org/10.1371/journal.ppat.0020113openalex-snapshot

Two Plasmodium Rhomboid Proteases Preferentially Cleave Different Adhesins Implicated in All Invasive Stages of Malaria

inferredcites →https://doi.org/10.1371/journal.ppat.1000262openalex-snapshot

Distinct Roles of Plasmodium Rhomboid 1 in Parasite Development and Malaria Pathogenesis

inferredcites →https://doi.org/10.1371/journal.ppat.1000858openalex-snapshot

Rhomboid 4 (ROM4) Affects the Processing of Surface Adhesins and Facilitates Host Cell Invasion by Toxoplasma gondii

inferredcites →https://doi.org/10.15252/embj.201489367openalex-snapshot

Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures

inferredcites →https://doi.org/10.15252/embj.201797909openalex-snapshot

PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria

inferredcites →https://doi.org/10.15252/embj.2019102935openalex-snapshot

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

inferredcites →https://doi.org/10.15252/embr.201642698openalex-snapshot

The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i‐AAA protease YME1L

inferredcites →https://doi.org/10.4161/auto.24633openalex-snapshot

PINK1 is degraded through the N-end rule pathway

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Extensive Targeting of Chemical Space at the Prime Side of Ketoamide Inhibitors of Rhomboid Proteases by Branched Substituents Empowers Their Selectivity and Potency

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Mitophagy and Ubiquitination Coordinate Context‐Specific Mitochondrial Quality Control and EMT/MET Plasticity to Drive Cancer Cell Invasion

inferred← citeshttps://doi.org/10.1002/ange.202514067openalex-snapshot

Targeting the Membrane‐Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight

inferred← citeshttps://doi.org/10.1002/anie.202514067openalex-snapshot

Targeting the Membrane‐Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight

inferred← citeshttps://doi.org/10.1007/s11686-026-01402-1openalex-snapshot

Rhomboid Proteases in Plasmodium spp. : Biology, Functional Roles, and Therapeutic Potential

inferred← citeshttps://doi.org/10.1007/s12035-026-05997-4openalex-snapshot

The Role of PINK1/Parkin-Mediated Mitophagy in Cerebral Ischemia-Reperfusion Injury: A Review of Recent Advances

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Hydrogel-based mitochondrial therapies: A new frontier in disease treatment

inferred← citeshttps://doi.org/10.1016/j.biopha.2023.115492openalex-snapshot

Contribution and therapeutic value of mitophagy in cerebral ischemia-reperfusion injury after cardiac arrest

inferred← citeshttps://doi.org/10.1016/j.ecoenv.2025.119239openalex-snapshot

Nitrite and microcystins co-exposure triggers PINK1-mediated mitophagy in spermatogonia

inferred← citeshttps://doi.org/10.1016/j.ejmech.2024.116606openalex-snapshot

Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency

inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108275openalex-snapshot

An in vitro platform for the enzymatic characterization of the rhomboid protease RHBDL4

inferred← citeshttps://doi.org/10.1016/j.tibs.2026.02.014openalex-snapshot

Molecular mechanisms of PINK1/Parkin-mediated mitochondrial quality control

inferred← citeshttps://doi.org/10.1021/acsmedchemlett.4c00384openalex-snapshot

4-Oxo-β-lactams as Covalent Inhibitors of the Mitochondrial Intramembrane Protease PARL

inferred← citeshttps://doi.org/10.1038/s41422-025-01203-7openalex-snapshot

Mitophagy in the pathogenesis and management of disease

inferred← citeshttps://doi.org/10.1038/s41467-025-60670-zopenalex-snapshot

Mitophagy mitigates mitochondrial fatty acid β-oxidation deficient cardiomyopathy

inferred← citeshttps://doi.org/10.1038/s41556-024-01513-9openalex-snapshot

The role of PINK1–Parkin in mitochondrial quality control

inferred← citeshttps://doi.org/10.1038/s41573-024-01105-0openalex-snapshot

Targeting mitophagy in neurodegenerative diseases

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Construction of prognostic markers for pancreatic adenocarcinoma based on mitochondrial fusion-related genes

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Electroacupuncture alleviates damage to myopic RGCs probably through lncRNA-XR_002789763.1-mediated mitophagy

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Mapping the global research landscape of mitophagy in Parkinson's disease: a bibliometric and visualization analysis

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The Mitophagy-Ferroptosis-Neuroinflammation Triad in Parkinson’s Disease: Pathogenic Crosstalk and Targeted Interventions

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Engineering cardiolipin binding to an artificial membrane protein reveals determinants for lipid-mediated stabilization

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Engineering cardiolipin binding to an artificial membrane protein reveals determinants for lipid-mediated stabilization

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Engineering cardiolipin binding to an artificial membrane protein reveals determinants for lipid-mediated stabilization

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Engineering cardiolipin binding to an artificial membrane protein reveals determinants for lipid-mediated stabilization

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