<scp>FXR</scp>
            proteins bring new perspectives to nucleoporins' homeostasis

Holzer, Guillaume; Antonin, Wolfram

doi:10.15252/embj.2020106510

Cited by 3 publications

(4 citation statements)

References 7 publications

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“…In the postmitotic pathway, NPC assembly occurs on segregated chromosomes, while during interphase, both Nup153 and POM121 drive de novo assembly of NPCs into an enclosed NE ( D’Angelo et al, 2006 ; Doucet et al, 2010 ; Vollmer et al, 2015 ), supported by several non-Nup assembly factors ( Dultz et al, 2022 ). The interphase pathway can be facilitated by FXR1 and microtubule-dependent transport of cytoplasmic Nups toward NE ( Agote-Aran et al, 2020 ; Agote-Arán et al, 2021 ; Holzer and Antonin, 2020 ). Given the strong interaction of UBAP2L with FXR1 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, defects in DNAJB6 and Ran induce annulate lamellae (AL) in the cytoplasm ( Walther et al, 2003b ; Kuiper et al, 2022 ), which are structures containing partly assembled NPCs embedded in the endoplasmic reticulum (ER) membrane sheets, a feature associated with perturbed NPC biogenesis ( Hampoelz et al, 2016 ). In addition to these well-established pathways, fragile X-related protein 1 (FXR1) was described to interact with Y-complex Nups in the cytoplasm and to facilitate their localization to the NE during interphase through a microtubule- and dynein-dependent mechanism, contributing to the NPC homeostasis during early interphase ( Agote-Aran et al, 2020 ; Agote-Arán et al, 2021 ; Holzer and Antonin, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

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UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope

Liao,

Andronov,

Liu

et al. 2024

Journal of Cell Biology

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Assembly of macromolecular complexes at correct cellular sites is crucial for cell function. Nuclear pore complexes (NPCs) are large cylindrical assemblies with eightfold rotational symmetry, built through hierarchical binding of nucleoporins (Nups) forming distinct subcomplexes. Here, we uncover a role of ubiquitin-associated protein 2-like (UBAP2L) in the assembly and stability of properly organized and functional NPCs at the intact nuclear envelope (NE) in human cells. UBAP2L localizes to the nuclear pores and facilitates the formation of the Y-complex, an essential scaffold component of the NPC, and its localization to the NE. UBAP2L promotes the interaction of the Y-complex with POM121 and Nup153, the critical upstream factors in a well-defined sequential order of Nups assembly onto NE during interphase. Timely localization of the cytoplasmic Nup transport factor fragile X-related protein 1 (FXR1) to the NE and its interaction with the Y-complex are likewise dependent on UBAP2L. Thus, this NPC biogenesis mechanism integrates the cytoplasmic and the nuclear NPC assembly signals and ensures efficient nuclear transport, adaptation to nutrient stress, and cellular proliferative capacity, highlighting the importance of NPC homeostasis at the intact NE.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope

Liao,

Andronov,

Liu

et al. 2024

Journal of Cell Biology

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“…Two distinct pathways of NPC assembly at the NE have been described during the cell cycle in higher eukaryotic cells (Weberruss & Antonin, 2016). In the postmitotic pathway, NPC assembly occurs on segregated chromosomes, while during interphase, both Nup153 and POM121 drive de novo assembly of NPCs into an enclosed NE (D'Angelo et al, 2006;Doucet et al, 2010;Vollmer et al, 2015), which can be facilitated by FXR1 and microtubule-dependent transport of cytoplasmic Nups towards NE (Agote-Aran et al, 2020;Agote-Arán et al, 2021;Holzer & Antonin, 2020). Given the strong interaction of UBAP2L with FXR1 (Fig.…”

Section: Ubap2l Regulates Localization Of Nups In Interphase But Not ...mentioning

confidence: 99%

“…Nup153 and POM121 are the critical upstream components in a well-defined sequential order of Nups assembly onto the interphase nuclei (Otsuka et al, 2016;Weberruss & Antonin, 2016). In addition, fragile X-related protein 1 (FXR1) can interact with cytoplasmic Y-complex Nups and facilitate their localization to the NE during interphase through a microtubule-and dynein-dependent mechanism, contributing to the NPC homeostasis (Agote-Aran et al, 2020;Agote-Arán et al, 2021;Holzer & Antonin, 2020).…”

Section: Introductionmentioning

confidence: 99%

UBAP2L drives scaffold assembly of nuclear pore complexes at the intact nuclear envelope

Liao,

Andronov,

Liu

et al. 2023

Preprint

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Assembly of macromolecular complexes at correct cellular sites is crucial for cell function. Nuclear pore complexes (NPCs) are large cylindrical assemblies with eightfold rotational symmetry, built through hierarchical binding of nucleoporins (Nups) forming distinct subcomplexes. Here, we uncover a direct role of ubiquitin-associated protein 2-like (UBAP2L) in the biogenesis of properly organized and functional NPCs at the intact nuclear envelope (NE) in human cells. UBAP2L localizes to the nuclear pores and drives the formation of the Y-complex, an essential scaffold component of the NPC, and its localization to the NE. UBAP2L facilitates the interaction of the Y-complex with POM121 and Nup153, the critical upstream factors in a well-defined sequential order of Nups assembly onto NE during interphase. Timely localization of the cytoplasmic Nup transport factor fragile X-related protein 1 (FXR1) to the NE and its interaction with the Y-complex are likewise dependent on UBAP2L. Thus, this NPC biogenesis mechanism integrates the cytoplasmic and the nuclear NPC assembly signals and ensures efficient nuclear transport, adaptation to nutrient stress and cellular proliferative capacity, highlighting the importance of NPC homeostasis at the intact nuclear envelope.TeaserLiao et al. show how UBAP2L drives the assembly of the scaffold elements into symmetrical and functional NPCs at the nuclear envelope in human cells.

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The multifaceted role of Fragile X-Related Protein 1 (FXR1) in cellular processes: an updated review on cancer and clinical applications

Khan,

Fang,

Zhang

et al. 2024

Cell Death Dis

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RNA-binding proteins (RBPs) modulate the expression level of several target RNAs (such as mRNAs) post-transcriptionally through interactions with unique binding sites in the 3′-untranslated region. There is mounting information that suggests RBP dysregulation plays a significant role in carcinogenesis. However, the function of FMR1 autosomal homolog 1(FXR1) in malignancies is just beginning to be unveiled. Due to the diversity of their RNA-binding domains and functional adaptability, FXR1 can regulate diverse transcript processing. Changes in FXR1 interaction with RNA networks have been linked to the emergence of cancer, although the theoretical framework defining these alterations in interaction is insufficient. Alteration in FXR1 expression or localization has been linked to the mRNAs of cancer suppressor genes, cancer-causing genes, and genes involved in genomic expression stability. In particular, FXR1-mediated gene regulation involves in several cellular phenomena related to cancer growth, metastasis, epithelial-mesenchymal transition, senescence, apoptosis, and angiogenesis. FXR1 dysregulation has been implicated in diverse cancer types, suggesting its diagnostic and therapeutic potential. However, the molecular mechanisms and biological effects of FXR1 regulation in cancer have yet to be understood. This review highlights the current knowledge of FXR1 expression and function in various cancer situations, emphasizing its functional variety and complexity. We further address the challenges and opportunities of targeting FXR1 for cancer diagnosis and treatment and propose future directions for FXR1 research in oncology. This work intends to provide an in-depth review of FXR1 as an emerging oncotarget with multiple roles and implications in cancer biology and therapy.

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FXR proteins bring new perspectives to nucleoporins' homeostasis

Cited by 3 publications

References 7 publications

UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope

UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope

UBAP2L drives scaffold assembly of nuclear pore complexes at the intact nuclear envelope

The multifaceted role of Fragile X-Related Protein 1 (FXR1) in cellular processes: an updated review on cancer and clinical applications

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