Ran-Binding Protein 3 Phosphorylation Links the Ras and PI3-Kinase Pathways to Nucleocytoplasmic Transport

Yoon, Sang-Oh; Shin, Sang Yong; Liu, Yuzhen; Ballif, Bryan A.; Woo, Michele S.; Gygi, Steven P.; Blenis, John

doi:10.1016/j.molcel.2007.12.024

Cited by 76 publications

(94 citation statements)

References 37 publications

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“…Given that RanBP3 is phosphoryated by RSK and Akt (Yoon et al, 2008), and influenza virus infection activates the Ras/ ERK and PI3K/Akt pathways, we sought to determine whether RanBP3 is activated during virus infection.…”

Section: Ranbp3 Is Activated During the Early And Late Phases Of Inflmentioning

confidence: 99%

“…These results suggested that the function of RanBP3 in vRNP export is regulated by phosphorylation at Ser58. Yoon et al (2008) reported that Ser58 is the only site in RanBP3 phosphorylated by the kinases RSK and Akt; phosphorylation at this site regulates nuclear export by modulating the Ran gradient across the cytoplasm and nucleus, in part by controlling RCC1 activity. More detailed study is required in the future to determine whether this is the mechanism by which RanBP3 phosphorylation regulates influenza vRNP nuclear export.…”

Section: Np Merge Dapi Wt Ranbp3mentioning

confidence: 99%

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The role of Ran-binding protein 3 during influenza A virus replication

Predicala

Zhou

2013

Journal of General Virology

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Influenza A virus vRNP nuclear export is CRM1-dependent. Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export. In this study, we investigated the role of RanBP3 during the influenza A virus life cycle. We found that RanBP3 was phosphorylated at Ser58 in the early and late phases of infection. Knockdown of RanBP3 expression led to vRNP nuclear retention, suggesting that RanBP3 is involved in vRNP nuclear export. Moreover, we demonstrated that the function of RanBP3 during vRNP nuclear export is regulated by phosphorylation at Ser58, and that RanBP3 phosphorylation is modulated by both PI3K/Akt and Ras/ERK/RSK pathways in the late phase of viral infection.

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Section: Ranbp3 Is Activated During the Early And Late Phases Of Inflmentioning

confidence: 99%

Section: Np Merge Dapi Wt Ranbp3mentioning

confidence: 99%

The role of Ran-binding protein 3 during influenza A virus replication

Predicala

Zhou

2013

Journal of General Virology

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“…Second, binding of RanBP3 to Crm1 increases the affinity of the latter for its cargos (Englmeier et al, 2001). Phosphorylation of RanBP3 by kinases such as Akt or Rsk stimulates its nuclear export activity (Yoon et al, 2008). Fragment N could favor NF-κB export by targeting the trimeric export complex.…”

Section: Discussionmentioning

confidence: 99%

The caspase-3/p120 RasGAP module generates a NF-κB repressor in response to cellular stress

Khalil

Loukili

Regamey

et al. 2015

Journal of Cell Science

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The nuclear factor κB (NF-κB) transcription factor is a master regulator of inflammation. Short-term NF-κB activation is generally beneficial. However, sustained NF-κB might be detrimental, directly causing apoptosis of cells or leading to a persistent damaging inflammatory response. NF-κB activity in stressed cells needs therefore to be controlled for homeostasis maintenance. In mildly stressed cells, caspase-3 cleaves p120 RasGAP, also known as RASA1, into an N-terminal fragment, which we call fragment N. We show here that this fragment is a potent NF-κB inhibitor. Fragment N decreases the transcriptional activity of NF-κB by promoting its export from the nucleus. Cells unable to generate fragment N displayed increased NF-κB activation upon stress. Knock-in mice expressing an uncleavable p120 RasGAP mutant showed exaggerated NF-κB activation when their epidermis was treated with anthralin, a drug used for the treatment of psoriasis. Our study provides biochemical and genetic evidence of the importance of the caspase-3-p120-RasGAP stress-sensing module in the control of stress-induced NF-κB activation.

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“…In addition to RCC1, RanGAP1 associated with RanBP2 is also phosphorylated by Cdks during mitotic progression (25). In addition, Ras/Akt signaling pathways modulate phosphorylation and function of RanBP3, which regulates the Ran gradient through control of RCC1 activity (32). RanBP1 is also regulated in order to ensure appropriate localization of mitotic regulatory factors on spindle microtubules and to perform chromosome segregation through modulation of RanGTP gradients during mitosis (31,45).…”

Section: Discussionmentioning

confidence: 99%

“…Ran-binding protein-3 (RanBP3), a member of the Ran-binding protein family, is phosphorylated by the Ras/ERK or PI3K/Akt signaling pathway. Phosphorylation of RanBP3 contributes to establishment of a Ran gradient and nucleocytoplasmic protein transport (32). Despite the dynamic functions of RanGTPase and its regulators, the clear mechanism of RanBP1 regulation in mammalian cells has not yet been eluci-dated.…”

mentioning

confidence: 99%

Phosphorylation of Ran-binding Protein-1 by Polo-like Kinase-1 Is Required for Interaction with Ran and Early Mitotic Progression

Hwang¹,

Ji²,

Jang

2011

Journal of Biological Chemistry

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Polo-like kinase-1 (Plk1) is essential for progression of mitosis and localizes to centrosomes, central spindles, midbody, and kinetochore. Ran, a small GTPase of the Ras superfamily, plays a role in microtubule dynamics and chromosome segregation during mitosis. Although Ran-binding protein-1 (RanBP1) has been reported as a regulator of RanGTPase for its mitotic functions, the action mechanism between Ran and RanBP1 during mitosis is still unknown. Here, we demonstrated in vitro and in vivo phosphorylation of RanBP1 by Plk1 as well as the importance of phosphorylation of RanBP1 in the interaction between Plk1 and Ran during early mitosis. Both phosphorylation-defective and N-terminal deletion mutant constructs of RanBP1 disrupted the interaction with Ran, and depletion of Plk1 also disrupted the formation of a complex between Ran and RanBP1. In addition, the results from both ectopic expression of phosphorylation-defective mutant construct and a functional complementation on RanBP1 deficiency with this mutant indicated that phosphorylation of RanBP1 by Plk1 might be crucial to microtubule nucleation and spindle assembly during mitosis.

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Ran-Binding Protein 3 Phosphorylation Links the Ras and PI3-Kinase Pathways to Nucleocytoplasmic Transport

Cited by 76 publications

References 37 publications

The role of Ran-binding protein 3 during influenza A virus replication

The role of Ran-binding protein 3 during influenza A virus replication

The caspase-3/p120 RasGAP module generates a NF-κB repressor in response to cellular stress

Phosphorylation of Ran-binding Protein-1 by Polo-like Kinase-1 Is Required for Interaction with Ran and Early Mitotic Progression

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