Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase

Yoon, Ina; Chung, Ji Hyung; Hahm, Soo Hyun; Park, Min Ju; Lee, You Ri; Ko, Sung Il; Kang, Lin Woo; Kim, Tae Sung; Kim, Joon; Han, Ye

doi:10.5483/bmbrep.2011.44.8.529

Cited by 23 publications

(22 citation statements)

References 22 publications

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“…For instance, RPs are phosphorylated throughout the mammalian cell cycle and contain the consensus kinase recognition site for CDK1 [19,42], a kinase that orchestrates essential steps of mitosis [42,43]. Additional evidence lies in work exploring CDK1 activity, which was found to phosphorylate Rps3/uS3 in vitro [44]. Interestingly, ribosome profiling across cell cycle stages revealed that specific transcripts are preferentially translated during different stages of the cell cycle, even though translation is globally repressed [45,46].…”

Section: Phosphorylated Ribosomes In Sickness and In Healthmentioning

confidence: 99%

An emerging role for the ribosome as a nexus for post-translational modifications

Şimşek

Barna

2017

Current Opinion in Cell Biology

111

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The ribosome is one of life’s most ancient molecular machines that has historically been viewed as a backstage participant in gene regulation, translating the genetic code across all kingdoms of life in a rote-like fashion. However, recent studies suggest that intrinsic components of the ribosome can be regulated and diversified as a means to intricately control the expression of the cellular proteome. In this review, we discuss advances in the characterization of ribosome post-translational modifications (PTMs) from past to present. We specifically focus on emerging examples of ribosome phosphorylation and ubiquitylation, which are beginning to showcase that PTMs of the ribosome are versatile, may have functional consequences for translational control, and are intimately linked to human disease. We further highlight the key questions that remain to be addressed to gain a more complete picture of the array of ribosome PTMs and the upstream enzymes that control them, which may endow ribosomes with greater regulatory potential in gene regulation and control of cellular homeostasis.

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Section: Phosphorylated Ribosomes In Sickness and In Healthmentioning

confidence: 99%

An emerging role for the ribosome as a nexus for post-translational modifications

Şimşek

Barna

2017

Current Opinion in Cell Biology

111

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“…We believe that this huge increase in protein phosphorylation at the start of mitosis is responsible for causing all of the structural changes associated with mitosis. Many other studies have identified hundreds of mitotic phosphoproteins, and most of them are likely phosphorylated by CDKs (10-12). However, much is still unclear about how these phosphorylation events are regulated and coordinated to ensure an ordered cell cycle progression.…”

Section: Introductionmentioning

confidence: 99%

PP2A function toward mitotic kinases and substrates during the cell cycle

Jeong

Yang

2013

BMB Reports

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To maintain cellular homeostasis against the demands of the extracellular environment, a precise regulation of kinases and phosphatases is essential. In cell cycle regulation mechanisms, activation of the cyclin-dependent kinase (CDK1) and cyclin B complex (CDK1:cyclin B) causes a remarkable change in protein phosphorylation. Activation of CDK1:cyclin B is regulated by two auto-amplification loops-CDK1:cyclin B activates Cdc25, its own activating phosphatase, and inhibits Wee1, its own inhibiting kinase. Recent biological evidence has revealed that the inhibition of its counteracting phosphatase activity also occurs, and it is parallel to CDK1:cyclin B activation during mitosis. Phosphatase regulation of mitotic kinases and their substrates is essential to ensure that the progression of the cell cycle is ordered. Outlining how the mutual control of kinases and phosphatases governs the localization and timing of cell division will give us a new understanding about cell cycle regulation. [BMB Reports 2013; 46(6): 289-294]

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“…This phosphorylation occurs at T221 and is important for the nuclear translocation of hRpS3 (21). Here, we studied the interaction between hRpS3 and Cdk2 (Fig.…”

Section: Discussionmentioning

confidence: 99%

New role of human ribosomal protein S3: Regulation of cell cycle via phosphorylation by cyclin-dependent kinase 2

et al. 2017

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Human ribosomal protein S3 (hRpS3) is a component of the 40S ribosomal subunit that associated in protein synthesis. hRpS3 has additional ribosomal functions such as DNA repair, transcription, metastasis, and apoptosis via interaction with numerous signaling molecules and has different modifications. Cyclin-dependent kinases (CDKs) are heterodimeric serine/threonine protein kinases that regulate cell cycle progression. Among its members, the Cdk1-cyclin B complex is known to control cell progression in the G2/M phase, while Cdk2-cyclin E/A complexes function in G1/S and S/G2 transition. In our previous study, we observed interaction between hRpS3 and Cdk1. The present study investigated the interaction between hRpS3 and Cdk2. Cdk2 phosphorylated hRps3 at amino acid residues S6 and T221 during the S-phase. Furthermore, hRpS3 knockdown delayed cell cycle progression by modulating the expression of cell cycle-related proteins, including cyclin B1 and cyclin E1. These findings suggest that hRpS3 is involved in Cdk2-mediated cell cycle regulation.

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Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase

Abstract: Ribosomal protein S3 (rpS3) is a multifunctional protein in

Cited by 23 publications

References 22 publications

An emerging role for the ribosome as a nexus for post-translational modifications

An emerging role for the ribosome as a nexus for post-translational modifications

PP2A function toward mitotic kinases and substrates during the cell cycle

New role of human ribosomal protein S3: Regulation of cell cycle via phosphorylation by cyclin-dependent kinase 2

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