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Current research on viral proteins that interact with fibrillarin
CARLO STEFANO DECLER CARRASCO
ALMA LAURA RODRIGUEZ PIÑA
Luis Carlos Rodríguez Zapata
Enrique Castaño de la Serna
Acceso Abierto
Atribución-NoComercial-SinDerivadas
https://doi.org/10.1007/s11033-023-08343-2
ANIMAL VIRUSES
FIBRILLARIN
HUMAN VIRUSES
INTRINSIC DISORDERED REGION
NUCLEOLUS
RIBOSOME BIOGENESIS
The nucleolus is a multifunctional nuclear domain primarily dedicated to ribosome biogenesis. Certain viruses developed strategies to manipulate host nucleolar proteins to facilitate their replication by modulating ribosomal RNA (rRNA) processing. This association interferes with nucleolar functions resulting in overactivation or arrest of ribosome biogenesis, induction or inhibition of apoptosis, and affecting stress response. The nucleolar protein fibrillarin (FBL) is an important target of some plant and animal viruses. FBL is an essential and highly conserved S-adenosyl methionine (SAM) dependent methyltransferase, capable of rRNA degradation by its intrinsically disordered region (IDR), the glycine/arginine-rich (GAR) domain. It forms a ribonucleoprotein complex that directs 2'-O-methylations in more than 100 sites of pre-rRNAs. It is involved in multiple cellular processes, including initiation of transcription, oncogenesis, and apoptosis, among others. The interaction with animal viruses, including human viruses, triggered its redistribution to the nucleoplasm and cytoplasm, interfering with its role in pre-rRNA processing. Viral-encoded proteins with IDRs as nucleocapsids, matrix, Tat protein, and even a viral snoRNA, can associate with FBL, forcing the nucleolar protein to undergo atypical functions. Here we review the molecular mechanisms employed by animal and human viruses to usurp FBL functions and the effect on cellular processes, particularly in ribosome biogenesis.
2023
Artículo
Mol Biol Rep. 2023 May;50(5):4631-4643, 2023.
Inglés
Decle-Carrasco S, Rodríguez-Piña AL, Rodríguez-Zapata LC, Castano E. Current research on viral proteins that interact with fibrillarin. Mol Biol Rep. 2023 May;50(5):4631-4643. doi: 10.1007/s11033-023-08343-2. Epub 2023 Mar 16. PMID: 36928641; PMCID: PMC10018631.
BIOLOGÍA MOLECULAR
Versión publicada
publishedVersion - Versión publicada
Aparece en las colecciones: Artículos de Investigación Arbitrados

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