De novo disruption of the proteasome regulatory subunit PSMD12 causes a syndromic neurodevelopmental disorder

Küry, Sébastien; Besnard, Thomas; Ebstein, Frédéric; Khan, Tahir N.; Gambin, Tomasz; Douglas, Jessica; Bacino, Carlos A.; Craigen, William J.; Sanders, Stephan J.; Lehmann, Andrea; Latypova, Xénia; Khan, Kamal; Pacault, Mathilde; Sacharow, Stephanie; Glaser, Kimberly; Bieth, Eric; Perrin-Sabourin, Laurence; Jacquemont, Marie-Line; Cho, Megan T.; Roeder, Elizabeth; Denommé-Pichon, Anne-Sophie; Monaghan, Kristin G.; Yuan, Bo; Xia, Fan; Simon, Sylvain; Bonneau, Dominique; Parent, Philippe; Gilbert-Dussardier, Brigitte; Odent, Sylvie; Toutain, Annick; Pasquier, Laurent; Barbouth, Deborah; Shaw, Chad A.; Patel, Ankita; Smith, Janice L.; Bi, Weimin; Schmitt, Sébastien; Deb, Wallid; Nizon, Mathilde; Mercier, Sandra; Vincent, Marie; Rooryck, Caroline; Malan, Valérie; Briceño, Ignacio; Gómez, Alberto; Nugent, Kimberly M.; Gibson, James B.; Cogné, Benjamin; Lupski, James R.; Stessman, Holly A.F.

doi:10.1016/j.ajhg.2017.01.003

Cited by 110Genetics and Neurodevelopmental DisordersUbiquitin and proteasome pathwaysGenomics and Rare Diseases

De novo disruption of the proteasome regulatory subunit PSMD12 causes a syndromic neurodevelopmental disorder

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Küry, Sébastien, Besnard, Thomas, Ebstein, Frédéric, Khan, Tahir N., Gambin, Tomasz, Douglas, Jessica, Bacino, Carlos A., Craigen, William J. +53 more·2017·The American Journal of Human Genetics

DOI 10.1016/j.ajhg.2017.01.003PMC PMC5294671

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Abstract

Degradation of proteins by the ubiquitin-proteasome system (UPS) is an essential biological process in the development of eukaryotic organisms. Dysregulation of this mechanism leads to numerous human neurodegenerative or neurodevelopmental disorders. Through a multi-center collaboration, we identified six de novo genomic deletions and four de novo point mutations involving PSMD12, encoding the non-ATPase subunit PSMD12 (aka RPN5) of the 19S regulator of 26S proteasome complex, in unrelated individuals with intellectual disability, congenital malformations, ophthalmologic anomalies, feeding difficulties, deafness, and subtle dysmorphic facial features. We observed reduced PSMD12 levels and an accumulation of ubiquitinated proteins without any impairment of proteasome catalytic activity. Our PSMD12 loss-of-function zebrafish CRISPR/Cas9 model exhibited microcephaly, decreased convolution of the renal tubules, and abnormal craniofacial morphology. Our data support the biological importance of PSMD12 as a scaffolding subunit in proteasome function during development and neurogenesis in particular; they enable the definition of a neurodevelopmental disorder due to PSMD12 variants, expanding the phenotypic spectrum of UPS-dependent disorders.

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These variants affect the protein levels of proteasome subunits, or decrease their incorporation into 20S and 26S proteasome and also the assembly of 20S and 26S proteasome.
“These variants affect the protein levels of proteasome subunits, or decreases their incorporation into 20S and 26S proteasome and also the assembly of 20S and 26S proteasome [18–20, 22, 23].”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [22]
The Figure 2 caption (p. 6) reports that a PSMD12 variant reduced full-length PSMD12 protein levels, supporting the protein-level part of the claim. But it explicitly says the 20S and 26S proteasome complexes were not altered. The discussion (p. 8) proposes decreased incorporation of RPN10 and RPN13 into the 26S proteasome as a possible explanation, not an established result; it does not show reduced incorporation into 20S proteasomes or impaired assembly of both complexes. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Mutations in genes encoding proteasome subunits result in neurodevelopmental disorders, as exemplified by variants in PSMB1, PSMC3, and PSMD12.
“Furthermore, mutations in genes encoding proteasome subunits result in neurodevelopmental disorders, as exemplified by variants of genes encoding the 20S CP subunit PSMB1 (β1) [18] and the 19S RP subunits PSMC3 [19, 20] and PSMD12 [21–23].”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [22]
Nonsense or missense variants of proteasome subunits PSMB1, PSMC3, and PSMD12 are associated with neurodevelopmental disorders.
“Previous published work has shown that nonsense or missense variants of proteasome subunits PSMB1 [18], PSMC3 [19, 20], and PSMD12 [22, 23] are associated with neurodevelopmental disorders.”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [22]

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Authors: Küry, S., Besnard, T., Ebstein, F., Khan, T. N., Gambin, T., Douglas, J., Bacino, C. A., Craigen, W. J., Sanders, S. J., Lehmann, A., Latypova, X., Khan, K., Pacault, M., Sacharow, S., Glaser, K., Bieth, E., Perrin-Sabourin, L., Jacquemont, M.-L., Cho, M. T., Roeder, E., Denommé-Pichon, A.-S., Monaghan, K. G., Yuan, B., Xia, F., Simon, S., Bonneau, D., Parent, P., Gilbert-Dussardier, B., Odent, S., Toutain, A., Pasquier, L., Barbouth, D., Shaw, C. A., Patel, A., Smith, J. L., Bi, W., Schmitt, S., Deb, W., Nizon, M., Mercier, S., Vincent, M., Rooryck, C., Malan, V., Briceño, I., Gómez, A., Nugent, K. M., Gibson, J. B., Cogné, B., Lupski, J. R., Stessman, H. A. F., Eichler, E. E., Retterer, K., Yang, Y., Redon, R., Katsanis, N., Rosenfeld, J. A., Kloetzel, P.-M., Golzio, C., Bézieau, S., Stankiewicz, P., & Isidor, B.
Affiliations: Centre Hospitalier Universitaire de Nantes (FR)
Charité – Universitätsmedizin Berlin (DE)
Duke Medical Center (US)
Warsaw University of Technology (PL)
Boston Children's Hospital (US)
Baylor College of Medicine (US)
University of California, San Francisco (US)
University of Miami (US)
Centre Hospitalier Universitaire de La Réunion (RE)
Inserm (FR)
Centre National de la Recherche Scientifique (FR)
Centre Hospitalier Régional Universitaire de Brest (FR)
Université de Tours (FR)
Centre Hospitalier Universitaire de Bordeaux (FR)
Hôpital Necker-Enfants Malades (FR)
Pontificia Universidad Javeriana (CO)
University of Washington (US)
Howard Hughes Medical Institute (US)
Duke University (US)
Corresponding author: Stankiewicz, Paweł
Isidor, Bertrand
ORCID: Küry, Sébastien
Besnard, Thomas
Ebstein, Frédéric
Khan, Tahir N.
Gambin, Tomasz
Bacino, Carlos A.
Sanders, Stephan J.
Lehmann, Andrea
Latypova, Xénia
Khan, Kamal
Pacault, Mathilde
Sacharow, Stephanie
Jacquemont, Marie-Line
Cho, Megan T.
Roeder, Elizabeth
Monaghan, Kristin G.
Yuan, Bo
Xia, Fan
Simon, Sylvain
Bonneau, Dominique
Odent, Sylvie
Toutain, Annick
Pasquier, Laurent
Shaw, Chad A.
Patel, Ankita
Smith, Janice L.
Bi, Weimin
Schmitt, Sébastien
Deb, Wallid
Nizon, Mathilde
Mercier, Sandra
Vincent, Marie
Rooryck, Caroline
Malan, Valérie
Briceño, Ignacio
Gómez, Alberto
Nugent, Kimberly M.
Cogné, Benjamin
Lupski, James R.
Stessman, Holly A.F.
Eichler, Evan E.
Retterer, Kyle
Yang, Yaping
Redon, Richard
Katsanis, Nicholas
Rosenfeld, Jill A.
Golzio, Christelle
Stankiewicz, Paweł
Isidor, Bertrand
Venue: The American Journal of Human Genetics
Publisher: Elsevier BV
Published: 2017-02
Volume: 100
Issue: 2
Pages: 352-363
ISSN: 0002-9297 (ISSN-L)
DOI: 10.1016/j.ajhg.2017.01.003
PMC: PMC5294671
OpenAlex: W2580973364
Cited by: 110
References: 63
Citations by year: 2026: 9 · 2025: 3 · 2024: 18 · 2023: 14 · 2022: 12 · 2021: 16 · 2020: 10 · 2019: 10 · 2018: 12 · 2017: 6
FWCI: 6.88
Type: journal article
Language: en
Update notices: erratum (2017-04-06)
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 182 d)
Locations: The American Journal of Human Genetics (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
eScholarship (California Digital Library) (submittedVersion)
Intellectum (Universidad de La Sabana) (submittedVersion, cc-by-nc-nd)
Repositorio Institucional (Pontificia Universidad Javeriana) (submittedVersion, cc-by-nc)
Funders: French Ministry of Health
Health Regional Agency from Poitou-Charentes (HUGODIMS, 2013, RC14_0107)
US National Human Genome Research Institute (U54HG006542)
National Heart, Lung, and Blood Institute
Wellcome Trust
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
Keywords: ubiquitin-proteasome system, de novo mutations, intellectual disability, neurodevelopmental disorders, syndromic disorders, microcephaly, craniofacial anomalies, loss of function, ubiquitinated protein accumulation, neurogenesis
MeSH terms: Adolescent, Animals, Child, Child, Preschool, Disease Models, Animal, Female, Humans, Infant, Male, Intellectual Disability, Microcephaly, Zebrafish, Down-Regulation, Gene Deletion, Polymorphism, Single Nucleotide, Proteasome Endopeptidase Complex, DNA Copy Number Variations, Neurodevelopmental Disorders

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De novo disruption of the proteasome regulatory subunit PSMD12 causes a syndromic neurodevelopmental disorder

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