HDGFL2 cryptic proteins report presence of TDP-43 pathology in neurodegenerative diseases.

Journal

Molecular neurodegeneration
ISSN: 1750-1326
Titre abrégé: Mol Neurodegener
Pays: England
ID NLM: 101266600

Informations de publication

Date de publication:
27 Mar 2024
Historique:
received: 09 02 2024
accepted: 11 03 2024
medline: 28 3 2024
pubmed: 28 3 2024
entrez: 28 3 2024
Statut: epublish

Résumé

This letter demonstrates the potential of novel cryptic proteins resulting from TAR DNA-binding protein 43 (TDP-43) dysfunction as markers of TDP-43 pathology in neurodegenerative diseases.

Identifiants

DOI: 10.1186/s13024-024-00718-8 PMID: 38539264
pubmed: 38539264
doi: 10.1186/s13024-024-00718-8
pii: 10.1186/s13024-024-00718-8
doi:

Types de publication

Letter

Langues

eng

Sous-ensembles de citation

IM

Pagination

29

Subventions

Organisme : NIA NIH HHS
ID : 5P30AG0062677
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : U19AG063911
Pays : United States
Organisme : NIA NIH HHS
ID : R01AG37491
Pays : United States
Organisme : NINDS NIH HHS
ID : U54NS123743
Pays : United States
Organisme : NINDS NIH HHS
ID : U54NS123743
Pays : United States
Organisme : NINDS NIH HHS
ID : U54NS123743
Pays : United States
Organisme : NINDS NIH HHS
ID : R35NS097273 (17,24)
Pays : United States
Organisme : NINDS NIH HHS
ID : R35NS097263(10,10)
Pays : United States
Organisme : NINDS NIH HHS
ID : P01NS084974
Pays : United States
Organisme : NINDS NIH HHS
ID : P01NS084974
Pays : United States
Organisme : NINDS NIH HHS
ID : P01NS084974
Pays : United States
Organisme : NINDS NIH HHS
ID : P01NS084974
Pays : United States
Organisme : NINDS NIH HHS
ID : RF1NS120992
Pays : United States
Organisme : NINDS NIH HHS
ID : RF1NS120992
Pays : United States
Organisme : NINDS NIH HHS
ID : R01NS117461
Pays : United States
Organisme : NINDS NIH HHS
ID : R01NS117461
Pays : United States
Organisme : NINDS NIH HHS
ID : R21NS127331
Pays : United States

Informations de copyright

© 2024. The Author(s).

Références

Ling JP, Pletnikova O, Troncoso JC, Wong PC. TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD. Science. 2015;349:650–5.
doi: 10.1126/science.aab0983 pubmed: 26250685 pmcid: 4825810
Brown AL, Wilkins OG, Keuss MJ, Hill SE, Zanovello M, Lee WC, Bampton A, Lee FCY, Masino L, Qi YA, et al. TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A. Nature. 2022;603:131–7.
doi: 10.1038/s41586-022-04436-3 pubmed: 35197628 pmcid: 8891020
Ma XR, Prudencio M, Koike Y, Vatsavayai SC, Kim G, Harbinski F, Briner A, Rodriguez CM, Guo C, Akiyama T, et al. TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A. Nature. 2022;603:124–30.
doi: 10.1038/s41586-022-04424-7 pubmed: 35197626 pmcid: 8891019
Melamed Z, Lopez-Erauskin J, Baughn MW, Zhang O, Drenner K, Sun Y, Freyermuth F, McMahon MA, Beccari MS, Artates JW, et al. Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration. Nat Neurosci. 2019;22:180–90.
doi: 10.1038/s41593-018-0293-z pubmed: 30643298 pmcid: 6348009
Klim JR, Williams LA, Limone F, Guerra San Juan I, Davis-Dusenbery BN, Mordes DA, Burberry A, Steinbaugh MJ, Gamage KK, Kirchner R, et al. ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair. Nat Neurosci. 2019;22:167–79.
doi: 10.1038/s41593-018-0300-4 pubmed: 30643292 pmcid: 7153761
Prudencio M, Humphrey J, Pickles S, Brown AL, Hill SE, Kachergus JM, Shi J, Heckman MG, Spiegel MR, Cook C, et al. Truncated stathmin-2 is a marker of TDP-43 pathology in frontotemporal dementia. J Clin Invest. 2020;130:6080–92.
doi: 10.1172/JCI139741 pubmed: 32790644 pmcid: 7598060
Estades Ayuso V, Pickles S, Todd T, Yue M, Jansen-West K, Song Y, Gonzalez Bejarano J, Rawlinson B, DeTure M, Graff-Radford NR, et al. TDP-43-regulated cryptic RNAs accumulate in Alzheimer’s disease brains. Mol Neurodegener. 2023;18:57.
doi: 10.1186/s13024-023-00646-z pubmed: 37605276 pmcid: 10441763
Chang K, Ling JP, Redding-Ochoa J, An Y, Li L, Dean SA, Blanchard TG, Pylyukh T, Barrett A, Irwin KE, et al. Loss of TDP-43 splicing repression occurs early in the aging population and is associated with Alzheimer’s disease neuropathologic changes and cognitive decline. Acta Neuropathol. 2023;147:4.
doi: 10.1007/s00401-023-02653-2 pubmed: 38133681
Chung M, Carter EK, Veire AM, Dammer EB, Chang J, Duong DM, Raj N, Bassell GJ, Glass JD, Gendron TF, et al. Cryptic exon inclusion is a molecular signature of LATE-NC in aging brains. Acta Neuropathol. 2024;147:29.
doi: 10.1007/s00401-023-02671-0 pubmed: 38308693 pmcid: 10838224
Seddighi S, Qi YA, Brown AL, Wilkins OG, Bereda C, Belair C, Zhang YJ, Prudencio M, Keuss MJ, Khandeshi A, et al. Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS/FTD. Sci Transl Med. 2024;16:eadg7162.
doi: 10.1126/scitranslmed.adg7162 pubmed: 38277467
Irwin KE, Jasin P, Braunstein KE, Sinha IR, Garret MA, Bowden KD, Chang K, Troncoso JC, Moghekar A, Oh ES, et al. A fluid biomarker reveals loss of TDP-43 splicing repression in presymptomatic ALS-FTD. Nat Med. 2024;30:382.
doi: 10.1038/s41591-023-02788-5 pubmed: 38278991 pmcid: 10878965
Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, Zidek A, Potapenko A, et al. Highly accurate protein structure prediction with AlphaFold. Nature. 2021;596:583–9.
doi: 10.1038/s41586-021-03819-2 pubmed: 34265844 pmcid: 8371605
Goddard TD, Huang CC, Meng EC, Pettersen EF, Couch GS, Morris JH, Ferrin TE. UCSF ChimeraX: Meeting modern challenges in visualization and analysis. Protein Sci. 2018;27:14–25.
doi: 10.1002/pro.3235 pubmed: 28710774
Coban MA, Morrison J, Maharjan S, Hernandez Medina DH, Li W, Zhang YS, Freeman WD, Radisky ES, Le Roch KG, Weisend CM, et al. Attacking COVID-19 progression using multi-drug therapy for synergetic target engagement. Biomolecules. 2021;11:787.
doi: 10.3390/biom11060787 pubmed: 34071060 pmcid: 8224684

Auteurs

Anna Calliari (A)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Lillian M Daughrity (LM)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Ellen A Albagli (EA)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Paula Castellanos Otero (P)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Mei Yue (M)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Karen Jansen-West (K)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Naeyma N Islam (NN)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Thomas Caulfield (T)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Bailey Rawlinson (B)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.

Michael DeTure (M)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.

Casey Cook (C)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.

Neill R Graff-Radford (NR)

Department of Neurology, Mayo Clinic, Jacksonville, FL, USA.

Gregory S Day (GS)

Department of Neurology, Mayo Clinic, Jacksonville, FL, USA.

Bradley F Boeve (BF)

Department of Neurology, Mayo Clinic, Rochester, MN, USA.

David S Knopman (DS)

Department of Neurology, Mayo Clinic, Rochester, MN, USA.

Ronald C Petersen (RC)

Department of Neurology, Mayo Clinic, Rochester, MN, USA.

Keith A Josephs (KA)

Department of Neurology, Mayo Clinic, Rochester, MN, USA.

Björn Oskarsson (B)

Department of Neurology, Mayo Clinic, Jacksonville, FL, USA.

Aaron D Gitler (AD)

Department of Genetics, Stanford University School of Medicine, Stanford, CA, USA.

Dennis W Dickson (DW)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.

Tania F Gendron (TF)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.

Mercedes Prudencio (M)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.

Michael E Ward (ME)

National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA. wardme@nih.gov.
Center for Alzheimer's and Related Dementias, National Institute on Aging and National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA. wardme@nih.gov.

Yong-Jie Zhang (YJ)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA. zhang.yongjie@mayo.edu.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA. zhang.yongjie@mayo.edu.

Leonard Petrucelli (L)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA. petrucelli.leonard@mayo.edu.
Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA. petrucelli.leonard@mayo.edu.
ORCID: 0000-0003-2959-129X

Classifications MeSH