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  1. Home
  2. Browse by Author

Browsing by Author "Lappala, Anna"

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    Revealing RCOR2 as a regulatory component of nuclear speckles
    (2021) Rivera Álvarez, Carlos Andrés; Verbel Vergara, Daniel Eduardo; Arancibia Radich, Duxan Andrés; Lappala, Anna; González, Marcela; Guzmán, Fabián; Merello, Gianluca; Lee, Jeannie T.; Andrés Coke, María Estela
    Background: Nuclear processes such as transcription and RNA maturation can be impacted by subnuclear compartmentalization in condensates and nuclear bodies. Here, we characterize the nature of nuclear granules formed by REST corepressor 2 (RCOR2), a nuclear protein essential for pluripotency maintenance and central nervous system development. Results: Using biochemical approaches and high-resolution microscopy, we reveal that RCOR2 is localized in nuclear speckles across multiple cell types, including neurons in the brain. RCOR2 forms complexes with nuclear speckle components such as SON, SRSF7, and SRRM2. When cells are exposed to chemical stress, RCOR2 behaves as a core component of the nuclear speckle and is stabilized by RNA. In turn, nuclear speckle morphology appears to depend on RCOR2. Specifically, RCOR2 knockdown results larger nuclear speckles, whereas overexpressing RCOR2 leads to smaller and rounder nuclear speckles. Conclusion: Our study suggests that RCOR2 is a regulatory component of the nuclear speckle bodies, setting this co-repressor protein as a factor that controls nuclear speckles behavior.
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    Unveiling RCOR1 as a rheostat at transcriptionally permissive chromatin
    (2022) Rivera, Carlos; Lee, Hun-Goo; Lappala, Anna; Wang, Danni; Noches, Veronica; Olivares-Costa, Montserrat; Sjoberg-Herrera, Marcela; Lee, Jeannie T.; Andres, Maria Estela
    The classical neuronal-gene corepressor RCOR1/CoREST is paradoxically enriched in transcriptionally active chromatin. Here the authors show RCOR1 is recruited during promoter-proximal pausing and negatively regulates the nascent-transcript synthesis. They also show that an RCOR1-LSD1- HDAC1 complex removes lysine acetylation from RNA polymerase II to repress transcription.

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