Erk phosphorylates threonine 42 residue of ribosomal protein S3

Kim, Hag Dong; Lee, Jae Yung; Kim, Joon

doi:10.1016/j.bbrc.2005.05.079

Cited by 33 publications

(28 citation statements)

References 30 publications

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“…This translocation appears to be dependent on the activation of ERK1/2, which in turn phosphorylates hS3 as part of the translocation process. The phosphorylation of hS3 is in agreement with previous results that showed that a threonine residue at position 42 is phosphorylated both in vitro and in vivo [30]. Furthermore, we have constructed site-directed mutants at T42 that blocks phosphorylation (T42A) and one that mimics constitutive phosphorylation (T42D).…”

Section: Discussionsupporting

confidence: 91%

“…Phosphorylation of ribosomal proteins often involve diverse classes of kinases that include PKC, CKII and ERK [28][29][30][31]. We therefore examined the effect that the inhibition of these kinases would have on hS3 translocation.…”

Section: Translocation Of Hs3 To the Nucleus Is Dependent Upon Erk1/2mentioning

confidence: 99%

“…As an alternative means of showing the dependence of hS3 translocation on phosphorylation by ERK1/2, we traced by immunofluorescence the subcellular localization of two different site directed mutants of the threonine residue at position 42 residing within the ERK1/2 phosphorylation motif of hS3 [30]. In the first case, threonine was mutated to alanine, and hS3 linked to GFP to form GFP-hS3-T42A.…”

Section: Translocation Of Hs3 To the Nucleus Is Dependent Upon Erk1/2mentioning

confidence: 99%

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Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

2007

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Besides its role in translation and ribosome maturation, human ribosomal protein S3 (hS3) is implicated in DNA damage recognition as reflected by its affinity for abasic sites and 7, 8-dihydro-8-oxoguanine (8-oxoG) residues in DNA in vitro. Here, we demonstrate that hS3 is capable of carrying out both roles by its ex vivo translocation from the cytoplasm to the nucleus as a consequence of genotoxic stress. The translocation of hS3 is dependent on ERK1/2-mediated phosphorylation of a threonine residue (T42) of hS3. Two different ectopically expressed site-directed mutants of T42 failed to respond to conditions of genotoxic stress, thus providing a link between DNA damage and ERK1/2 dependent phosphorylation of hS3. Lastly, hS3 was traced in exposed cells to its colocalization with 8-oxoG foci, raising the possibility that hS3 is a member of a cellular DNA damage response pathway that results in its interaction with sites of DNA damage.

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Section: Discussionsupporting

confidence: 91%

Section: Translocation Of Hs3 To the Nucleus Is Dependent Upon Erk1/2mentioning

confidence: 99%

Section: Translocation Of Hs3 To the Nucleus Is Dependent Upon Erk1/2mentioning

confidence: 99%

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Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

2007

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“…Plant roots typically contain proplastids, some of which can be changed into chloroplasts after exposure to light (Oliveira 1982). S3 protein is involved in the synthesis of small ribosomal subunit (30S) and in the repair of DNA damage (Kim et al 2005). S3 may also function as a transcription factor (Wan et al 2007).…”

Section: Discussionmentioning

confidence: 99%

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

2013

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Osmotic stress causes many adverse symptoms in plants, which include, for example, growth limitation and decrease or even absence of yield. Proteomic analyses of plant responses to stressors could lead to the introduction of crops with high resistance to osmotic stress. Such plants would be characterized by high yield even under unfavorable environmental conditions. In this article we describe changes in the protein profiles occurring in response to mild and moderate osmotic stress in triticale roots. Analysis of the protein profiles of these roots showed an increased abundance of 14 and a decreased abundance of 11 proteins under mild osmotic stress conditions while a moderate osmotic stress caused an increased abundance of 18 and a decreased abundance of 33 proteins. Twenty-five proteins, whose quantity altered under stress were identified using MALDI-TOF mass spectrometry. The identified proteins were classified into the categories of proteins associated with: defense mechanisms, metabolism, transcription, cell structure, protein synthesis, transport and signal transduction. The functions of identified proteins were discussed in relation to osmotic stress. Some of the identified proteins may be responsible for the adaptation of plants to adverse conditions.

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“…62 Moreover, the phosphorylation of the T42 residue of RPS3 by ERK facilitates its nuclear entry. 63 The precise role of NleH2 in ERK/MAPK pathways, whether via the ERK substrate RPS3 or independent of RPS3, requires more investigation. Overall, NleD, NleC and NleH2 have been implicated in signaling regulation from the perspective of MAPK (Figure 1).…”

Section: Mapk Inflammatory Signaling Pathwaysmentioning

confidence: 99%

Modulation of host signaling in the inflammatory response by enteropathogenic Escherichia coli virulence proteins

Zhuang

Chen

et al. 2016

Cell Mol Immunol

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To successfully infect host cells and evade the host immune response, a type III secretion system (T3SS) is commonly used by enteric bacterial pathogens such as enteropathogenic Escherichia coli (EPEC). Recent findings have revealed that various effectors are injected into host cells through the T3SS and exert an inhibitory effect on inflammatory signaling pathways, subverting the immune responses to these pathogens. Here we review recent studies aimed at addressing the modulation of several important inflammatory signaling pathways modulated by EPEC effector proteins, such as the nuclear factor-κB (NF-κB) and mitogen-activated protein kinase (MAPK) pathways, which provides insight into the unfinished work in this unexplored field and helps to identify novel positions in inflammatory signaling networks for EPEC effectors.

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Erk phosphorylates threonine 42 residue of ribosomal protein S3

Cited by 33 publications

References 30 publications

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

Changes in the root proteome of Triticosecale grains germinating under osmotic stress

Modulation of host signaling in the inflammatory response by enteropathogenic Escherichia coli virulence proteins

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