IronSulferCluV1, Main, Exploration, bibRecord, 000179

Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.

Identifieur interne : 000179 ( Main/Exploration ); précédent : 000178; suivant : 000180

Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.

Auteurs : Nima N. Naseri [États-Unis] ; Burçe Ergel [États-Unis] ; Parinati Kharel [États-Unis] ; Yoonmi Na [États-Unis] ; Qingqiu Huang [États-Unis] ; Rong Huang [États-Unis] ; Natalia Dolzhanskaya [États-Unis] ; Jacqueline Burré [États-Unis] ; Milen T. Velinov [États-Unis] ; Manu Sharma [États-Unis]

Source :

Nature structural & molecular biology [ 1545-9985 ] ; 2020.

RBID : pubmed:32042150

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Cells, Cultured (MeSH), Female (MeSH), HEK293 Cells (MeSH), HSP40 Heat-Shock Proteins (genetics), HSP40 Heat-Shock Proteins (metabolism), Humans (MeSH), Iron Chelating Agents (metabolism), Lipoylation (MeSH), Membrane Proteins (genetics), Membrane Proteins (metabolism), Mice (MeSH), Neuronal Ceroid-Lipofuscinoses (genetics), Neuronal Ceroid-Lipofuscinoses (metabolism), Neurons (metabolism), Point Mutation (MeSH), Protein Aggregation, Pathological (genetics), Protein Aggregation, Pathological (metabolism), Protein Binding (MeSH), Protein Multimerization (MeSH).
MESH :
- chemical , genetics : HSP40 Heat-Shock Proteins, Membrane Proteins.
- chemical , metabolism : HSP40 Heat-Shock Proteins, Iron Chelating Agents, Membrane Proteins.
- genetics : Neuronal Ceroid-Lipofuscinoses, Protein Aggregation, Pathological.
- metabolism : Neuronal Ceroid-Lipofuscinoses, Neurons, Protein Aggregation, Pathological.
- Animals, Cells, Cultured, Female, HEK293 Cells, Humans, Lipoylation, Mice, Point Mutation, Protein Binding, Protein Multimerization.

Abstract

Point mutations in cysteine string protein-α (CSPα) cause dominantly inherited adult-onset neuronal ceroid lipofuscinosis (ANCL), a rapidly progressing and lethal neurodegenerative disease with no treatment. ANCL mutations are proposed to trigger CSPα aggregation/oligomerization, but the mechanism of oligomer formation remains unclear. Here we use purified proteins, mouse primary neurons and patient-derived induced neurons to show that the normally palmitoylated cysteine string region of CSPα loses palmitoylation in ANCL mutants. This allows oligomerization of mutant CSPα via ectopic binding of iron-sulfur (Fe-S) clusters. The resulting oligomerization of mutant CSPα causes its mislocalization and consequent loss of its synaptic SNARE-chaperoning function. We then find that pharmacological iron chelation mitigates the oligomerization of mutant CSPα, accompanied by partial rescue of the downstream SNARE defects and the pathological hallmark of lipofuscin accumulation. Thus, the iron chelators deferiprone (L1) and deferoxamine (Dfx), which are already used to treat iron overload in humans, offer a new approach for treating ANCL.

DOI: 10.1038/s41594-020-0375-y
PubMed: 32042150
PubMed Central: PMC7021000

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Cells, Cultured (MeSH)</term>
<term>Female (MeSH)</term>
<term>HEK293 Cells (MeSH)</term>
<term>HSP40 Heat-Shock Proteins (genetics)</term>
<term>HSP40 Heat-Shock Proteins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron Chelating Agents (metabolism)</term>
<term>Lipoylation (MeSH)</term>
<term>Membrane Proteins (genetics)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Mice (MeSH)</term>
<term>Neuronal Ceroid-Lipofuscinoses (genetics)</term>
<term>Neuronal Ceroid-Lipofuscinoses (metabolism)</term>
<term>Neurons (metabolism)</term>
<term>Point Mutation (MeSH)</term>
<term>Protein Aggregation, Pathological (genetics)</term>
<term>Protein Aggregation, Pathological (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Agents chélateurs du fer (métabolisme)</term>
<term>Agrégation pathologique de protéines (génétique)</term>
<term>Agrégation pathologique de protéines (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Cellules HEK293 (MeSH)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Céroïdes-lipofuscinoses neuronales (génétique)</term>
<term>Céroïdes-lipofuscinoses neuronales (métabolisme)</term>
<term>Femelle (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Lipoylation (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
<term>Mutation ponctuelle (MeSH)</term>
<term>Neurones (métabolisme)</term>
<term>Protéines du choc thermique HSP40 (génétique)</term>
<term>Protéines du choc thermique HSP40 (métabolisme)</term>
<term>Protéines membranaires (génétique)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Souris (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>HSP40 Heat-Shock Proteins</term>
<term>Membrane Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HSP40 Heat-Shock Proteins</term>
<term>Iron Chelating Agents</term>
<term>Membrane Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Neuronal Ceroid-Lipofuscinoses</term>
<term>Protein Aggregation, Pathological</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Agrégation pathologique de protéines</term>
<term>Céroïdes-lipofuscinoses neuronales</term>
<term>Protéines du choc thermique HSP40</term>
<term>Protéines membranaires</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neuronal Ceroid-Lipofuscinoses</term>
<term>Neurons</term>
<term>Protein Aggregation, Pathological</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Agents chélateurs du fer</term>
<term>Agrégation pathologique de protéines</term>
<term>Céroïdes-lipofuscinoses neuronales</term>
<term>Neurones</term>
<term>Protéines du choc thermique HSP40</term>
<term>Protéines membranaires</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cells, Cultured</term>
<term>Female</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Lipoylation</term>
<term>Mice</term>
<term>Point Mutation</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules HEK293</term>
<term>Cellules cultivées</term>
<term>Femelle</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Lipoylation</term>
<term>Multimérisation de protéines</term>
<term>Mutation ponctuelle</term>
<term>Souris</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Point mutations in cysteine string protein-α (CSPα) cause dominantly inherited adult-onset neuronal ceroid lipofuscinosis (ANCL), a rapidly progressing and lethal neurodegenerative disease with no treatment. ANCL mutations are proposed to trigger CSPα aggregation/oligomerization, but the mechanism of oligomer formation remains unclear. Here we use purified proteins, mouse primary neurons and patient-derived induced neurons to show that the normally palmitoylated cysteine string region of CSPα loses palmitoylation in ANCL mutants. This allows oligomerization of mutant CSPα via ectopic binding of iron-sulfur (Fe-S) clusters. The resulting oligomerization of mutant CSPα causes its mislocalization and consequent loss of its synaptic SNARE-chaperoning function. We then find that pharmacological iron chelation mitigates the oligomerization of mutant CSPα, accompanied by partial rescue of the downstream SNARE defects and the pathological hallmark of lipofuscin accumulation. Thus, the iron chelators deferiprone (L1) and deferoxamine (Dfx), which are already used to treat iron overload in humans, offer a new approach for treating ANCL.</div>
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<Title>Nature structural & molecular biology</Title>
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<ArticleTitle>Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.</ArticleTitle>
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<Abstract><AbstractText>Point mutations in cysteine string protein-α (CSPα) cause dominantly inherited adult-onset neuronal ceroid lipofuscinosis (ANCL), a rapidly progressing and lethal neurodegenerative disease with no treatment. ANCL mutations are proposed to trigger CSPα aggregation/oligomerization, but the mechanism of oligomer formation remains unclear. Here we use purified proteins, mouse primary neurons and patient-derived induced neurons to show that the normally palmitoylated cysteine string region of CSPα loses palmitoylation in ANCL mutants. This allows oligomerization of mutant CSPα via ectopic binding of iron-sulfur (Fe-S) clusters. The resulting oligomerization of mutant CSPα causes its mislocalization and consequent loss of its synaptic SNARE-chaperoning function. We then find that pharmacological iron chelation mitigates the oligomerization of mutant CSPα, accompanied by partial rescue of the downstream SNARE defects and the pathological hallmark of lipofuscin accumulation. Thus, the iron chelators deferiprone (L1) and deferoxamine (Dfx), which are already used to treat iron overload in humans, offer a new approach for treating ANCL.</AbstractText>
</Abstract>
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<ForeName>Burçe</ForeName>
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<AffiliationInfo><Affiliation>Appel Institute for Alzheimer's Disease Research, and Brain & Mind Research Institute, Weill Cornell Medicine, New York, NY, USA.</Affiliation>
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<ForeName>Parinati</ForeName>
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   |texte=   Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.
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Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.

Aggregation of mutant cysteine string protein-α via Fe-S cluster binding is mitigated by iron chelators.

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