Deciphering the role of Zn2+‐binding histidines from TIA‐1 on the assembly and dynamics of stress granules.
| Title: | Deciphering the role of Zn2+‐binding histidines from TIA‐1 on the assembly and dynamics of stress granules. |
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| Authors: | Corrales‐Guerrero, Laura1 (AUTHOR) laucorge@us.es, Díaz‐Moreno, Irene1 (AUTHOR) idiazmoreno@us.es |
| Source: | Biofactors. Jul2024, Vol. 50 Issue 4, p750-755. 6p. |
| Subject Terms: | *RNA-binding proteins, *STRESS granules, *AMYOTROPHIC lateral sclerosis, *PHASE separation, *GENETIC translation, *RNA splicing |
| Abstract: | T‐cell intracellular antigen‐1 (TIA‐1) is a key RNA‐binding protein that participates in translation regulation and RNA splicing. TIA‐1 undergoes liquid–liquid phase separation as a fundamental mechanism that enables the condensation of RNA and proteins into membraneless organelles called stress granules (SGs). However, this dynamic behavior can lead to aberrant fibril formation, implicated in neurodegenerative disorders, and must be tightly regulated. In this study, we investigated the role in the cell of histidine residues His94 and His96, responsible for Zn2+ binding. Using fluorescence microscopy, we found that the specific binding site formed by these residues is critical for SG assembly. Furthermore, it also plays a role maintaining the dynamic behavior of SG‐assembled TIA‐1. Collectively, our findings confirm the physiological relevance of TIA‐1 His94 and His96 in the Zn2+‐mediated regulatory mechanism for protection against fibril formation in SGs. [ABSTRACT FROM AUTHOR] |
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| Items | – Name: Title Label: Title Group: Ti Data: Deciphering the role of Zn<superscript>2+</superscript>‐binding histidines from TIA‐1 on the assembly and dynamics of stress granules. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Corrales‐Guerrero%2C+Laura%22">Corrales‐Guerrero, Laura</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> laucorge@us.es</i><br /><searchLink fieldCode="AR" term="%22Díaz‐Moreno%2C+Irene%22">Díaz‐Moreno, Irene</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> idiazmoreno@us.es</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biofactors%22">Biofactors</searchLink>. Jul2024, Vol. 50 Issue 4, p750-755. 6p. – Name: Subject Label: Subject Terms Group: Su Data: *<searchLink fieldCode="DE" term="%22RNA-binding+proteins%22">RNA-binding proteins</searchLink><br />*<searchLink fieldCode="DE" term="%22STRESS+granules%22">STRESS granules</searchLink><br />*<searchLink fieldCode="DE" term="%22AMYOTROPHIC+lateral+sclerosis%22">AMYOTROPHIC lateral sclerosis</searchLink><br />*<searchLink fieldCode="DE" term="%22PHASE+separation%22">PHASE separation</searchLink><br />*<searchLink fieldCode="DE" term="%22GENETIC+translation%22">GENETIC translation</searchLink><br />*<searchLink fieldCode="DE" term="%22RNA+splicing%22">RNA splicing</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: T‐cell intracellular antigen‐1 (TIA‐1) is a key RNA‐binding protein that participates in translation regulation and RNA splicing. TIA‐1 undergoes liquid–liquid phase separation as a fundamental mechanism that enables the condensation of RNA and proteins into membraneless organelles called stress granules (SGs). However, this dynamic behavior can lead to aberrant fibril formation, implicated in neurodegenerative disorders, and must be tightly regulated. In this study, we investigated the role in the cell of histidine residues His94 and His96, responsible for Zn2+ binding. Using fluorescence microscopy, we found that the specific binding site formed by these residues is critical for SG assembly. Furthermore, it also plays a role maintaining the dynamic behavior of SG‐assembled TIA‐1. Collectively, our findings confirm the physiological relevance of TIA‐1 His94 and His96 in the Zn2+‐mediated regulatory mechanism for protection against fibril formation in SGs. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biofactors is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1002/biof.2037 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 6 StartPage: 750 Subjects: – SubjectFull: RNA-binding proteins Type: general – SubjectFull: STRESS granules Type: general – SubjectFull: AMYOTROPHIC lateral sclerosis Type: general – SubjectFull: PHASE separation Type: general – SubjectFull: GENETIC translation Type: general – SubjectFull: RNA splicing Type: general Titles: – TitleFull: Deciphering the role of Zn2+‐binding histidines from TIA‐1 on the assembly and dynamics of stress granules. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Corrales‐Guerrero, Laura – PersonEntity: Name: NameFull: Díaz‐Moreno, Irene IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 07 Text: Jul2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 09516433 Numbering: – Type: volume Value: 50 – Type: issue Value: 4 Titles: – TitleFull: Biofactors Type: main |
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