Centromere protein W interacts with beta‐transducin repeat‐containing protein 1 and modulates its subcellular localization

Cheon, Yeongmi; Jeon, Seyeong; Lee, Soo Jin

doi:10.1002/1873-3468.12483

Cited by 5 publications

(5 citation statements)

References 24 publications

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“…We identified that CSN-5 interacts with CENP-W and modulates CENP-W protein stability (10). Another of our studies revealed that CENP-W binds with b-TrCP-1 and contributes its nucleocytoplasmic shuttling (11), which raises the possibility that CENP-W is functionally related to the SCF b-TrCP-1 complex. In the current study, we provide evidence that CENP-W associates with SCF b-TrCP-1 components by replacing SKP-1 and inhibiting its ubiquitin ligase activity, suggesting that CENP-W is a new regulator that contributes to the fine tuning of SCF b-TrCP-1 E3 ligase activity.…”

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confidence: 71%

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CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M

Cheon

Lee

2018

FASEB j.

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Skp, Cullin, F-box (SCF) ubiquitin ligases play a central role in cell cycle regulation and tumorigenesis via proteolytic cleavage of many essential cell cycle regulators. In this study, we propose that centromere protein (CENP)-W, a newly identified kinetochore component, is a novel negative regulator of the SCF complex. CENP-W interacts with Cullin (CUL)-1 and β-Transducin repeat-containing protein (β-TrCP)-1 through highly overlapped binding sites with S-phase kinase-associated protein (SKP)-1. CENP-W is incorporated into the SCF complex to promote complex disassembly. Unlike other known regulators that increase SCF ubiquitin ligase activity by promoting complex reassociation, CENP-W-mediated complex disorganization induced β-TrCP1 degradation and consequently decreased its activity. The association between CENP-W and the SCF complex was prominent during the G/M transition in the nucleus. Especially, CENP-W knockdown decreased the cell division cycle-25A protein level, leading to a delay in mitotic progression. We propose that CENP-W participates in cell cycle regulation by modulating SCF ubiquitin ligase activity.-Cheon, Y., Lee, S. CENP-W inhibits CDC25A degradation by destabilizing the SCF complex at G/M.

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confidence: 71%

“…Our prior study revealed that CENP-W interacts with b-TrCP1 and contributes to its nuclear translocation (11). To clarify the specificity of this interaction, we performed a binding assay with other F-box family proteins.…”

Section: Cenp-w Associates With B-trcp1 By Replacing Skp1mentioning

confidence: 99%

CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M

Cheon

Lee

2018

FASEB j.

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“…It has been shown that hnRNP‐U, HIV‐1 Vpu, and TRIM9 compete with β‐TrCP1 for substrates binding, thereby limiting the β‐TrCP1 E3 ligase activity [41–43]. Further, it has been reported that centromere protein CENP‐W regulates shuttling of β‐TrCP1 between the cytoplasm and the nucleus [44]. CENP‐W also destabilizes β‐TrCP1 E3 ligase complex resulting in degradation [45].…”

Section: Discussionmentioning

confidence: 99%

FBXW8 regulates G1 and S phases of cell cycle progression by restricting β‐TrCP1 function

et al. 2021

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Sequential alteration in the expression levels of cell cycle regulatory proteins is crucial for faithful cell cycle progression to maintain the cellular homeostasis. F‐box protein β‐TrCP1 is known to control the expression levels of several important cell cycle regulatory proteins. However, how the function of β‐TrCP1 is regulated in spatiotemporal manner during cell cycle progression remains elusive. Here, we show that expression levels of β‐TrCP1 oscillate during cell cycle progression with a minimum level at the G1 and S phases of cell cycle. Using biochemical, flow cytometry, and immunofluorescence techniques, we found that oscillation of β‐TrCP1 expression is controlled by another F‐box protein FBXW8. FBXW8 directs the proteasomal degradation of β‐TrCP1 in MAPK pathway‐dependent manner. Interestingly, we found that the attenuation of β‐TrCP1 by FBXW8 is important for Cdc25A‐mediated cell cycle transition from G1 phase to S phase as well as DNA damage‐free progression of S phase. Overall, our study reveals the intriguing molecular mechanism and significance of maintenance of β‐TrCP1 levels during cell cycle progression by FBXW8‐mediated proteasomal degradation.

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“…Centromere protein W (CENP-W) and heterogeneous nuclear ribonucleoprotein U (hnRNP U) interact with the region of F box and the WD40 domain of β-TrCP1, respectively [122]. The interaction complex leads to a stable shuttling complex, resulting in the accumulation of β-TrCP1 in the nucleus and promoting cell migration.…”

Section: Regulation Of β-Trcp Activity 61 Upstream Effectors Of β-Trc...mentioning

confidence: 99%

“…The interaction complex leads to a stable shuttling complex, resulting in the accumulation of β-TrCP1 in the nucleus and promoting cell migration. It has been proposed that CENP-W may enhance the oncogenic potential of β-TrCP1 by promoting its nuclear accumulation [122].…”

Section: Regulation Of β-Trcp Activity 61 Upstream Effectors Of β-Trc...mentioning

confidence: 99%

Beta-Transducin Repeats-Containing Proteins as an Anticancer Target

Kim,

Yi,

Seong

2023

Cancers

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Beta-transducin repeat-containing proteins (β-TrCPs) are E3-ubiquitin-ligase-recognizing substrates and regulate proteasomal degradation. The degradation of β-TrCPs’ substrates is tightly controlled by various external and internal signaling and confers diverse cellular processes, including cell cycle progression, apoptosis, and DNA damage response. In addition, β-TrCPs function to regulate transcriptional activity and stabilize a set of substrates by distinct mechanisms. Despite the association of β-TrCPs with tumorigenesis and tumor progression, studies on the mechanisms of the regulation of β-TrCPs’ activity have been limited. In this review, we studied publications on the regulation of β-TrCPs themselves and analyzed the knowledge gaps to understand and modulate β-TrCPs’ activity in the future.

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Centromere protein W interacts with beta‐transducin repeat‐containing protein 1 and modulates its subcellular localization

Cited by 5 publications

References 24 publications

CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M

CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M

FBXW8 regulates G1 and S phases of cell cycle progression by restricting β‐TrCP1 function

Beta-Transducin Repeats-Containing Proteins as an Anticancer Target

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Centromere protein W interacts with beta‐transducin repeat‐containing protein 1 and modulates its subcellular localization

Cited by 5 publications

References 24 publications

CENP‐W inhibits CDC25A degradation by destabilizing the SCF β‐TrCP‐1 complex at G 2 /M

CENP‐W inhibits CDC25A degradation by destabilizing the SCF β‐TrCP‐1 complex at G 2 /M

FBXW8 regulates G1 and S phases of cell cycle progression by restricting β‐TrCP1 function

Beta-Transducin Repeats-Containing Proteins as an Anticancer Target

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CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M

CENP‐W inhibits CDC25A degradation by destabilizing the SCF ^{β‐TrCP‐1} complex at G ₂ /M