Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy.

Autoproteolysis CAPN5 Calpain-5 Membrane NIV Palmitoylation S-acylation

Journal

Biochimica et biophysica acta. Molecular basis of disease
ISSN: 1879-260X
Titre abrégé: Biochim Biophys Acta Mol Basis Dis
Pays: Netherlands
ID NLM: 101731730

Informations de publication

Date de publication:
08 2023
Historique:
received: 22 07 2022
revised: 29 03 2023
accepted: 02 05 2023
pmc-release: 01 08 2024
medline: 5 6 2023
pubmed: 20 5 2023
entrez: 19 5 2023
Statut: ppublish

Résumé

Neovascular inflammatory vitreoretinopathy (NIV) is a rare eye disease that ultimately leads to complete blindness and is caused by mutations in the gene encoding calpain-5 (CAPN5), with six pathogenic mutations identified. In transfected SH-SY5Y cells, five of the mutations resulted in decreased membrane association, diminished S-acylation, and reduced calcium-induced autoproteolysis of CAPN5. CAPN5 proteolysis of the autoimmune regulator AIRE was impacted by several NIV mutations. R243, L244, K250 and the adjacent V249 are on β-strands in the protease core 2 domain. Conformational changes induced by Ca

Identifiants

pubmed: 37207905
pii: S0925-4439(23)00113-8
doi: 10.1016/j.bbadis.2023.166747
pmc: PMC10332796
mid: NIHMS1905445
pii:
doi:

Substances chimiques

Calpain EC 3.4.22.-
Capn5 protein, human EC 3.4.22.-

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

166747

Subventions

Organisme : NINDS NIH HHS
ID : R01 NS095229
Pays : United States

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: James W. Geddes reports financial support was provided by National Institutes of Health.

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Auteurs

James W Geddes (JW)

Spinal Cord and Brain Injury Research Center (SCoBIRC), University of Kentucky, Lexington, KY 40536, USA; Department of Neuroscience, University of Kentucky, Lexington, KY 40536, USA. Electronic address: jgeddes@uky.edu.

Vimala Bondada (V)

Spinal Cord and Brain Injury Research Center (SCoBIRC), University of Kentucky, Lexington, KY 40536, USA.

Dorothy E Croall (DE)

Department of Molecular and Biomedical Sciences, University of Maine, Orono, ME 04469, USA. Electronic address: croall@maine.edu.

David W Rodgers (DW)

Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA. Electronic address: david.rodgers@uky.edu.

Jozsef Gal (J)

Spinal Cord and Brain Injury Research Center (SCoBIRC), University of Kentucky, Lexington, KY 40536, USA; Department of Neuroscience, University of Kentucky, Lexington, KY 40536, USA. Electronic address: jgal2@uky.edu.

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Classifications MeSH