The autophagy of stress granules

Ryan, Laura; Rubinsztein, David C.

doi:10.1002/1873-3468.14787

Cited by 7 publications

(3 citation statements)

References 139 publications

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“…1A; 1B) 7,8 , forms reversible stress granules (SGs). SGs are biomolecular condensates composed of RNAs and proteins when the cell is under stress 1,9,10 . Particularly, the morphology of intracellular Rim4 changes from a mesh-like diffusion state to a spatially concentrated pattern under multiple stress conditions such as PH decrease in sporulation medium (PH 5.5) and oxidative stress (0.5% NaN 3 ) but primarily by heat (37°C) (Fig.…”

Section: Main Textmentioning

confidence: 99%

Rim4 is a Thermal Sensor and Driver of Meiosis-specific Stress Granules

Zhang,

Li,

Feng

et al. 2024

Preprint

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Rim4 is a meiosis-specific RNA-binding protein (RBP) that sequesters mRNAs to suppress their translation. Previous work has defined the Rim4 C-terminal low-complexity domain (LCD) as sequences that form self-propagating amyloid-like aggregates. Here, we uncovered a dynamic and reversible form of Rim4 self-assembly primarily triggered by heat during meiosis, proportionally from 30°C to 42°C. The formed thermal Rim4 condensates in cell promptly stimulates stress granule (SG) assembly, recruiting SG-resident proteins, such as Pab1 and Pbp1, and strikingly, decreases the required temperature for meiotic SG formation (~33°C) by ~9°C as compared to mitosis (~42°C). This sensitization of meiotic SG formation to heat effectively prevents meiosis progression and sporulation under harmful thermal turbulence. Meanwhile, the Rim4-positive meiotic SGs protect Rim4 and Rim4-sequestered mRNAs from autophagy to allow a rapid recovery from stalled meiosis upon the stress relief. Mechanistically, we found that the yeast 14-3-3 proteins (Bmh1 and Bmh2) and nucleic acids brake initiation of heat-induced Rim4 self-assembly, and Hsp104 facilitates the restoration of intracellular Rim4 distribution during the recovery.

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Section: Main Textmentioning

confidence: 99%

Rim4 is a Thermal Sensor and Driver of Meiosis-specific Stress Granules

Zhang,

Li,

Feng

et al. 2024

Preprint

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“…The presence of RNA-binding proteins and RNA is critical for stress granule assembly and liquid-liquid phase separation (LLPS). The intrinsically disordered regions (IDRs) of RNA-binding proteins, such as G3BP1, TIA-1, CAPRIN1, and FMRP, contribute to LLPS and stress granule nucleation [60][61][62]. UBAP2L is an interacting protein of FMRP and is thought to be a core protein in SGs [63,64].…”

Section: Stress Granules Formationmentioning

confidence: 99%

Fragile X Messenger Ribonucleoprotein Protein and Its Multifunctionality: From Cytosol to Nucleolus and Back

Taha,

Ahmadian

2024

Biomolecules

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Silencing of the fragile X messenger ribonucleoprotein 1 (FMR1) gene and a consequent lack of FMR protein (FMRP) synthesis are associated with fragile X syndrome, one of the most common inherited intellectual disabilities. FMRP is a multifunctional protein that is involved in many cellular functions in almost all subcellular compartments under both normal and cellular stress conditions in neuronal and non-neuronal cell types. This is achieved through its trafficking signals, nuclear localization signal (NLS), nuclear export signal (NES), and nucleolar localization signal (NoLS), as well as its RNA and protein binding domains, and it is modulated by various post-translational modifications such as phosphorylation, ubiquitination, sumoylation, and methylation. This review summarizes the recent advances in understanding the interaction networks of FMRP with a special focus on FMRP stress-related functions, including stress granule formation, mitochondrion and endoplasmic reticulum plasticity, ribosome biogenesis, cell cycle control, and DNA damage response.

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“…SGs can interact with autophagic machinery, either being engulfed by autophagosomes themselves or releasing their cargo to be processed by autophagy. 53 , 217 Targeting these interactions could potentially open up new avenues for therapeutic intervention in cancer progression where SG dynamics are disrupted.…”

Section: Molecular Functions Of Stress Granules In Cancer Biologymentioning

confidence: 99%