Shuttling of cellular proteins between the plasma membrane and nucleus (Review)

Hua-chuan, Zheng; Jiang, Huamao

doi:10.3892/mmr.2021.12530

Cited by 11 publications

(13 citation statements)

References 94 publications

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“…Active communication between the cell cortex and the nucleus is important to ensure a coordinated transcriptional response upon extracellular stimuli (Zheng & Jiang, 2022). Among the proteins that participate in the FAs, zyxin, paxillin and FAK have been shown to translocate to the nucleus and regulate gene expression (Wang & Gilmore, 2003; Lim et al , 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Active communication between the cell cortex and the nucleus is important to ensure a coordinated transcriptional response upon extracellular stimuli (Zheng & Jiang, 2022).…”

Section: C)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Accumulating evidence indicates active communication between the cell cortex and the nucleus by nuclear translocation of proteins (Zheng & Jiang, 2022). Many of these proteins are associated with transmembrane adhesion receptors, which connect the extracellular matrix (ECM) and surface proteins of neighboring cells to the cytoskeleton (Hintermann & Christen, 2019; Zheng & Jiang, 2022). These cell-ECM and cell-cell junctions provide cells with structural and mechanical stability, and both types of junctions act as signaling platforms that collect information from the extracellular space.…”

Section: Introductionmentioning

confidence: 99%

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A subpopulation of Talin 1 resides in the nucleus and regulates gene expression

Silva

Hästbacka

Puustinen

et al. 2022

Preprint

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Talin 1 (TLN1) is best known for its role at focal adhesions, where it activates β-integrin receptors and transmits mechanical stimuli to the actin cytoskeleton. Interestingly, the localization of TLN1 is not restricted to the focal adhesions, but its function in other cellular compartments remains poorly understood. By utilizing both biochemical and confocal microscopy analyses, we show that TLN1 localizes to the nucleus and that it strongly interacts with the chromatin. Importantly, depletion of endogenous TLN1 results in extensive changes in the gene expression profile of human breast epithelial cells. To determine the impact of nuclear TLN1 on gene regulation, we expressed a TLN1 fusion protein containing a nuclear localization signal. Our results revealed that nuclear TLN1 regulates a specific subset of the TLN1-dependent genes. Taken together, we show that apart from localizing at the plasma membrane and cytoplasm, TLN1 also resides in the nucleus where it functions in the regulation of gene expression.

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Section: Discussionmentioning

confidence: 99%

“…Active communication between the cell cortex and the nucleus is important to ensure a coordinated transcriptional response upon extracellular stimuli (Zheng & Jiang, 2022).…”

Section: C)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A subpopulation of Talin 1 resides in the nucleus and regulates gene expression

Silva

Hästbacka

Puustinen

et al. 2022

Preprint

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“…These include proteins that make up focal adhesions, adherens junctions, tight junctions, gap junctions, and desmosomes ( Figure 1B and Table 1 ). These cell adhesion proteins, which typically participate in either signal reception and/or short-term responses, are increasingly recognized as also being localized in the nucleus ( Figure 1C ) and directly participating in gene regulation, a classic long-term response, without the need for intermediary signal transducers ( Hervy et al, 2006 ; Zuleger et al, 2012 ; Zheng and Jiang, 2022 ). This observation further breaks down the division of labor between molecules that function at relatively short versus long timescales.…”

Section: Introductionmentioning

confidence: 99%

Working a second job: Cell adhesion proteins that moonlight in the nucleus

Haage

Dhasarathy

2023

Front. Cell Dev. Biol.

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Cells are adept at sensing changes in their environment, transmitting signals internally to coordinate responses to external stimuli, and thereby influencing adaptive changes in cell states and behavior. Often, this response involves modulation of gene expression in the nucleus, which is seen largely as a physically separated process from the rest of the cell. Mechanosensing, whereby a cell senses physical stimuli, and integrates and converts these inputs into downstream responses including signaling cascades and gene regulatory changes, involves the participation of several macromolecular structures. Of note, the extracellular matrix (ECM) and its constituent macromolecules comprise an essential part of the cellular microenvironment, allowing cells to interact with each other, and providing both structural and biochemical stimuli sensed by adhesion transmembrane receptors. This highway of information between the ECM, cell adhesion proteins, and the cytoskeleton regulates cellular behavior, the disruption of which results in disease. Emerging evidence suggests a more direct role for some of these adhesion proteins in chromatin structure and gene regulation, RNA maturation and other non-canonical functions. While many of these discoveries were previously limited to observations of cytoplasmic-nuclear transport, recent advances in microscopy, and biochemical, proteomic and genomic technologies have begun to significantly enhance our understanding of the impact of nuclear localization of these proteins. This review will briefly cover known cell adhesion proteins that migrate to the nucleus, and their downstream functions. We will outline recent advances in this very exciting yet still emerging field, with impact ranging from basic biology to disease states like cancer.

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