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  1. Article ; Online: A point mutation in human coilin prevents Cajal body formation.

    Basello, Davide A / Matera, A Gregory / Staněk, David

    Journal of cell science

    2022  Volume 135, Issue 8

    Abstract: Coilin is a conserved protein essential for integrity of nuclear membrane-less inclusions called Cajal bodies. Here, we report an amino acid substitution (p.K496E) found in a widely-used human EGFP-coilin construct that has a dominant-negative effect on ... ...

    Abstract Coilin is a conserved protein essential for integrity of nuclear membrane-less inclusions called Cajal bodies. Here, we report an amino acid substitution (p.K496E) found in a widely-used human EGFP-coilin construct that has a dominant-negative effect on Cajal body formation. We show that this coilin-K496E variant fails to rescue Cajal bodies in cells lacking endogenous coilin, whereas the wild-type construct restores Cajal bodies in mouse and human coilin-knockout cells. In cells containing endogenous coilin, both the wild-type and K496E variant proteins accumulate in Cajal bodies. However, high-level overexpression of coilin-K496E causes Cajal body disintegration. Thus, a mutation in the C-terminal region of human coilin can disrupt Cajal body assembly. Caution should be used when interpreting data from coilin plasmids that are derived from this variant (currently deposited at Addgene).
    MeSH term(s) Animals ; Coiled Bodies/genetics ; HeLa Cells ; Humans ; Mice ; Mutation/genetics ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Point Mutation/genetics
    Chemical Substances Nuclear Proteins
    Language English
    Publishing date 2022-04-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.259587
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  2. Article ; Online: Lysine-36 of Drosophila histone H3.3 supports adult longevity.

    Brown, John C / McMichael, Benjamin D / Vandadi, Vasudha / Mukherjee, Aadit / Salzler, Harmony R / Matera, A Gregory

    G3 (Bethesda, Md.)

    2024  Volume 14, Issue 4

    Abstract: Aging is a multifactorial process that disturbs homeostasis, increases disease susceptibility, and ultimately results in death. Although the definitive set of molecular mechanisms responsible for aging remain to be discovered, epigenetic change over time ...

    Abstract Aging is a multifactorial process that disturbs homeostasis, increases disease susceptibility, and ultimately results in death. Although the definitive set of molecular mechanisms responsible for aging remain to be discovered, epigenetic change over time is proving to be a promising piece of the puzzle. Several post-translational histone modifications have been linked to the maintenance of longevity. Here, we focus on lysine-36 of the replication-independent histone protein, H3.3 (H3.3K36). To interrogate the role of this residue in Drosophila developmental gene regulation, we generated a lysine-to-arginine mutant that blocks the activity of its cognate-modifying enzymes. We found that an H3.3BK36R mutation causes a significant reduction in adult lifespan, accompanied by dysregulation of the genomic and transcriptomic architecture. Transgenic co-expression of wild-type H3.3B completely rescues the longevity defect. Because H3.3 is known to accumulate in nondividing tissues, we carried out transcriptome profiling of young vs aged adult fly heads. The data show that loss of H3.3K36 results in age-dependent misexpression of NF-κB and other innate immune target genes, as well as defects in silencing of heterochromatin. We propose H3.3K36 maintains the postmitotic epigenomic landscape, supporting longevity by regulating both pericentric and telomeric retrotransposons and by suppressing aberrant immune signaling.
    MeSH term(s) Animals ; Drosophila/genetics ; Drosophila/metabolism ; Heterochromatin ; Histones/genetics ; Histones/metabolism ; Longevity/genetics ; Lysine/metabolism
    Chemical Substances Heterochromatin ; Histones ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2024-02-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2629978-1
    ISSN 2160-1836 ; 2160-1836
    ISSN (online) 2160-1836
    ISSN 2160-1836
    DOI 10.1093/g3journal/jkae030
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  3. Article ; Online: Twenty years of RNA: reflections from the RNP world.

    Matera, A Gregory

    RNA (New York, N.Y.)

    2015  Volume 21, Issue 4, Page(s) 690–691

    MeSH term(s) RNA/chemistry ; RNA/genetics ; Ribonucleoproteins/chemistry
    Chemical Substances Ribonucleoproteins ; RNA (63231-63-0)
    Language English
    Publishing date 2015-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.050153.115
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  4. Article ; Online: Dysregulation of innate immune signaling in animal models of spinal muscular atrophy.

    Garcia, Eric L / Steiner, Rebecca E / Raimer, Amanda C / Herring, Laura E / Matera, A Gregory / Spring, Ashlyn M

    BMC biology

    2024  Volume 22, Issue 1, Page(s) 94

    Abstract: Background: Spinal muscular atrophy (SMA) is a devastating neuromuscular disease caused by hypomorphic loss of function in the survival motor neuron (SMN) protein. SMA presents across a broad spectrum of disease severity. Unfortunately, genetic models ... ...

    Abstract Background: Spinal muscular atrophy (SMA) is a devastating neuromuscular disease caused by hypomorphic loss of function in the survival motor neuron (SMN) protein. SMA presents across a broad spectrum of disease severity. Unfortunately, genetic models of intermediate SMA have been difficult to generate in vertebrates and are thus unable to address key aspects of disease etiology. To address these issues, we developed a Drosophila model system that recapitulates the full range of SMA severity, allowing studies of pre-onset biology as well as late-stage disease processes.
    Results: Here, we carried out transcriptomic and proteomic profiling of mild and intermediate Drosophila models of SMA to elucidate molecules and pathways that contribute to the disease. Using this approach, we elaborated a role for the SMN complex in the regulation of innate immune signaling. We find that mutation or tissue-specific depletion of SMN induces hyperactivation of the immune deficiency (IMD) and Toll pathways, leading to overexpression of antimicrobial peptides (AMPs) and ectopic formation of melanotic masses in the absence of an external challenge. Furthermore, the knockdown of downstream targets of these signaling pathways reduced melanotic mass formation caused by SMN loss. Importantly, we identify SMN as a negative regulator of a ubiquitylation complex that includes Traf6, Bendless, and Diap2 and plays a pivotal role in several signaling networks.
    Conclusions: In alignment with recent research on other neurodegenerative diseases, these findings suggest that hyperactivation of innate immunity contributes to SMA pathology. This work not only provides compelling evidence that hyperactive innate immune signaling is a primary effect of SMN depletion, but it also suggests that the SMN complex plays a regulatory role in this process in vivo. In summary, immune dysfunction in SMA is a consequence of reduced SMN levels and is driven by cellular and molecular mechanisms that are conserved between insects and mammals.
    MeSH term(s) Animals ; Muscular Atrophy, Spinal/genetics ; Muscular Atrophy, Spinal/immunology ; Immunity, Innate ; Disease Models, Animal ; Signal Transduction ; Drosophila melanogaster/immunology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism
    Chemical Substances Drosophila Proteins
    Language English
    Publishing date 2024-04-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2133020-7
    ISSN 1741-7007 ; 1741-7007
    ISSN (online) 1741-7007
    ISSN 1741-7007
    DOI 10.1186/s12915-024-01888-z
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  5. Article ; Online: tRNA introns: Presence, processing, and purpose.

    Schmidt, Casey A / Matera, A Gregory

    Wiley interdisciplinary reviews. RNA

    2019  Volume 11, Issue 3, Page(s) e1583

    Abstract: The presence of introns in both protein-coding and noncoding RNA transcripts is a fascinating phenomenon. It seems counterintuitive that an organism would devote precious time and energy to removing a nucleic acid sequence that will not be present in the ...

    Abstract The presence of introns in both protein-coding and noncoding RNA transcripts is a fascinating phenomenon. It seems counterintuitive that an organism would devote precious time and energy to removing a nucleic acid sequence that will not be present in the final product. Nevertheless, introns (including self-splicing ones) are clearly important components of the basic cellular process of gene expression. Transfer RNA (tRNA) introns have been detected in all three kingdoms of life, and their precise removal is crucial for tRNA function. Of particular interest to this review are the tRNA intronic circular RNAs (tricRNAs) that form during metazoan tRNA splicing. In animal cells, these ultrastable introns form a novel class of noncoding RNA. Here, we summarize established knowledge and describe new findings in the field of tRNA splicing. This article is categorized under: RNA Processing > Splicing Mechanisms RNA Structure and Dynamics > Influence of RNA Structure in Biological Systems RNA in Disease and Development > RNA in Disease RNA Processing > tRNA Processing.
    MeSH term(s) Animals ; Humans ; Introns ; Nucleic Acid Conformation ; RNA Splicing/genetics ; RNA, Transfer/genetics ; RNA, Untranslated/genetics
    Chemical Substances RNA, Untranslated ; RNA, Transfer (9014-25-9)
    Language English
    Publishing date 2019-12-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2634714-3
    ISSN 1757-7012 ; 1757-7004
    ISSN (online) 1757-7012
    ISSN 1757-7004
    DOI 10.1002/wrna.1583
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  6. Article ; Online: Author Correction: Structural basis for pre-tRNA recognition and processing by the human tRNA splicing endonuclease complex.

    Hayne, Cassandra K / Butay, Kevin John U / Stewart, Zachary D / Krahn, Juno M / Perera, Lalith / Williams, Jason G / Petrovitch, Robert M / Deterding, Leesa J / Matera, A Gregory / Borgnia, Mario J / Stanley, Robin E

    Nature structural & molecular biology

    2024  Volume 31, Issue 2, Page(s) 390

    Language English
    Publishing date 2024-01-09
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-024-01213-w
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  7. Article: Lysine-36 of

    Brown, John C / McMichael, Benjamin D / Vandadi, Vasudha / Mukherjee, Aadit / Salzler, Harmony R / Matera, A Gregory

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Aging is a multifactorial process that disturbs homeostasis, increases disease susceptibility, and ultimately results in death. Although the definitive set of molecular mechanisms responsible for aging remain to be discovered, epigenetic change over time ...

    Abstract Aging is a multifactorial process that disturbs homeostasis, increases disease susceptibility, and ultimately results in death. Although the definitive set of molecular mechanisms responsible for aging remain to be discovered, epigenetic change over time is proving to be a promising piece of the puzzle. Several posttranslational histone modifications (PTMs) have been linked to the maintenance of longevity. Here, we focus on lysine-36 of the replication-independent histone protein, H3.3 (H3.3K36). To interrogate the role of this residue in
    Language English
    Publishing date 2023-12-13
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.09.28.559962
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  8. Article: Dysregulation of innate immune signaling in animal models of Spinal Muscular Atrophy.

    Garcia, Eric L / Steiner, Rebecca E / Raimer, Amanda C / Herring, Laura E / Matera, A Gregory / Spring, Ashlyn M

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Background: Spinal Muscular Atrophy (SMA) is a devastating neuromuscular disease caused by hypomorphic loss of function in the Survival Motor Neuron (SMN) protein. SMA presents across broad spectrum of disease severity. Unfortunately, vertebrate models ... ...

    Abstract Background: Spinal Muscular Atrophy (SMA) is a devastating neuromuscular disease caused by hypomorphic loss of function in the Survival Motor Neuron (SMN) protein. SMA presents across broad spectrum of disease severity. Unfortunately, vertebrate models of intermediate SMA have been difficult to generate and are thus unable to address key aspects of disease etiology. To address these issues, we developed a
    Results: Here, we carried out transcriptomic and proteomic profiling of mild and intermediate
    Conclusions: In alignment with recent research on other neurodegenerative diseases, these findings suggest that hyperactivation of innate immunity contributes to SMA pathology. This work not only provides compelling evidence that hyperactive innate immune signaling is a primary effect of SMN depletion, but it also suggests that the SMN complex plays a regulatory role in this process
    Language English
    Publishing date 2023-12-15
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.12.14.571739
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: A homozygous missense variant in the YG box domain in an individual with severe spinal muscular atrophy: a case report and variant characterization.

    Li, Leping / Perera, Lalith / Varghese, Sonia A / Shiloh-Malawsky, Yael / Hunter, Senyene E / Sneddon, Tam P / Powell, Cynthia M / Matera, A Gregory / Fan, Zheng

    Frontiers in cellular neuroscience

    2023  Volume 17, Page(s) 1259380

    Abstract: The vast majority of severe (Type 0) spinal muscular atrophy (SMA) cases are caused by homozygous deletions of survival motor neuron 1 ( ...

    Abstract The vast majority of severe (Type 0) spinal muscular atrophy (SMA) cases are caused by homozygous deletions of survival motor neuron 1 (
    Language English
    Publishing date 2023-09-26
    Publishing country Switzerland
    Document type Case Reports
    ZDB-ID 2452963-1
    ISSN 1662-5102
    ISSN 1662-5102
    DOI 10.3389/fncel.2023.1259380
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  10. Article: Gemin4

    Meier, Ingo D / Walker, Michael P / Matera, A Gregory

    Biology open

    2018  Volume 7, Issue 2

    Abstract: Gemin4 is a member of the Survival Motor Neuron (SMN) protein complex, which is responsible for the assembly and maturation of Sm-class small nuclear ribonucleoproteins (snRNPs). In metazoa, Sm snRNPs are assembled in the cytoplasm and subsequently ... ...

    Abstract Gemin4 is a member of the Survival Motor Neuron (SMN) protein complex, which is responsible for the assembly and maturation of Sm-class small nuclear ribonucleoproteins (snRNPs). In metazoa, Sm snRNPs are assembled in the cytoplasm and subsequently imported into the nucleus. We previously showed that the SMN complex is required for snRNP import
    Language English
    Publishing date 2018-02-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 2632264-X
    ISSN 2046-6390
    ISSN 2046-6390
    DOI 10.1242/bio.032409
    Database MEDical Literature Analysis and Retrieval System OnLINE

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