ΔNp63<i>α</i> controls <scp>YB</scp>‐1 protein stability: evidence on <scp>YB</scp>‐1 as a new player in keratinocyte differentiation

Martino, Orsola di; Troiano, Annaelena; Guarino, Andrea Maria; Pollice, Alessandra; Vivo, Maria; Mantia, Girolama La; Calabrò, Viola

doi:10.1111/gtc.12373

Cited by 24 publications

(21 citation statements)

References 25 publications

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“…Consistent with previous studies where multiple YB-1 immunoreactive bands were associated with complex post translational modifications [27, 31, 33], we also observed differences in the number and molecular weight of immunoreactive bands depending on the antibody used (ranging between 45 and 60 kDa). In addition, the oscillation of nuclear YB-1 expression persisted under constant conditions (constant darkness, DD) showing a circadian clock regulation rather than simply a light-dependent YB-1 rhythmicity (Figure 2C and Supplementary Figure S2D and Supplementary Table S1).…”

Section: Resultssupporting

confidence: 91%

The tumor-associated YB-1 protein: new player in the circadian control of cell proliferation

et al. 2016

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Correct spatial and temporal control of cell proliferation is of fundamental importance for tissue homeostasis. Its deregulation has been associated with several pathological conditions. In common with almost every aspect of plant and animal biology, cell proliferation is dominated by day-night rhythms generated by the circadian clock. However, our understanding of the crosstalk between the core clock and cell cycle control mechanisms remains incomplete. In this study, using zebrafish as a vertebrate model system, we show that the nuclear localization of the Y-box binding protein 1 (YB-1), a regulator of cyclin expression and a hallmark of certain cancers, is robustly regulated by the circadian clock. We implicate clock-controlled changes in YB-1 SUMOylation as one of the mechanisms regulating its periodic nuclear entry at the beginning of the light phase. Furthermore, we demonstrate that YB-1 nuclear protein is able to downregulate cyclin A2 mRNA expression in zebrafish via its direct interaction with the cyclin A2 promoter. Thus, by acting as a direct target of cyclic posttranslational regulatory mechanisms, YB-1 serves as one bridge between the circadian clock and its cell cycle control.

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Section: Resultssupporting

confidence: 91%

The tumor-associated YB-1 protein: new player in the circadian control of cell proliferation

et al. 2016

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“…It is documented that the functions played by YB-1 are strictly dependent on its subcellular localization [ 16 , 39 , 40 ]. Thus, we examined YB-1 subcellular localization in human HEK293T cells in resting conditions and following treatment with Na Ars, a well-known inducer of oxidative stress and translational arrest [ 41 , 42 ].…”

Section: Resultsmentioning

confidence: 99%

“…We have previously demonstrated that intracellular YB-1 is implicated in keratinocytes proliferation and survival to oxidative stress [ 40 , 48 ]. To get an insight into the function of secreted YB-1 we evaluated the proliferative response of HaCaT cells to the addition of rYB-1 or HPLC-purified YB-1 from HEK293T cell culture medium (CCM-YB-1).…”

Section: Resultsmentioning

confidence: 99%

Oxidative Stress Causes Enhanced Secretion of YB-1 Protein that Restrains Proliferation of Receiving Cells

Guarino

Troiano

Pizzo

et al. 2018

Genes

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The prototype cold-shock Y-box binding protein 1 (YB-1) is a multifunctional protein that regulates a variety of fundamental biological processes including cell proliferation and migration, DNA damage, matrix protein synthesis and chemotaxis. The plethora of functions assigned to YB-1 is strictly dependent on its subcellular localization. In resting cells, YB-1 localizes to cytoplasm where it is a component of messenger ribonucleoprotein particles. Under stress conditions, YB-1 contributes to the formation of stress granules (SGs), cytoplasmic foci where untranslated messenger RNAs (mRNAs) are sorted or processed for reinitiation, degradation, or packaging into ribonucleoprotein particles (mRNPs). Following DNA damage, YB-1 translocates to the nucleus and participates in DNA repair thereby enhancing cell survival. Recent data show that YB-1 can also be secreted and YB-1-derived polypeptides are found in plasma of patients with sepsis and malignancies. Here we show that in response to oxidative insults, YB-1 assembly in SGs is associated with an enhancement of YB-1 protein secretion. An enriched fraction of extracellular YB-1 (exYB-1) significantly inhibited proliferation of receiving cells and such inhibition was associated to a G2/M cell cycle arrest, induction of p21WAF and reduction of ΔNp63α protein level. All together, these data show that acute oxidative stress causes sustained release of YB-1 as a paracrine/autocrine signal that stimulate cell cycle arrest.

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“…YB-1 can also be secreted [ 88 ]. Acetylation and ubiquitination of YB-1 have both been shown to play roles in regulating secretion as well as intracellular stability [ 58 , 90 , 107 , 108 ]. YB-1 can be proteolytically cleaved and extracellular YB-1, and/or fragments thereof, is found in the serum of patients, binds to cell surface receptors, and exerts extracellular activities, e.g.…”

Section: Cold Shock Proteins In Diseasementioning

confidence: 99%

Cold shock proteins: from cellular mechanisms to pathophysiology and disease

2018

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Cold shock proteins are multifunctional RNA/DNA binding proteins, characterized by the presence of one or more cold shock domains. In humans, the best characterized members of this family are denoted Y-box binding proteins, such as Y-box binding protein-1 (YB-1). Biological activities range from the regulation of transcription, splicing and translation, to the orchestration of exosomal RNA content. Indeed, the secretion of YB-1 from cells via exosomes has opened the door to further potent activities. Evidence links a skewed cold shock protein expression pattern with cancer and inflammatory diseases. In this review the evidence for a causative involvement of cold shock proteins in disease development and progression is summarized. Furthermore, the potential application of cold shock proteins for diagnostics and as targets for therapy is elucidated.

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ΔNp63α controls YB‐1 protein stability: evidence on YB‐1 as a new player in keratinocyte differentiation

Cited by 24 publications

References 25 publications

The tumor-associated YB-1 protein: new player in the circadian control of cell proliferation

The tumor-associated YB-1 protein: new player in the circadian control of cell proliferation

Oxidative Stress Causes Enhanced Secretion of YB-1 Protein that Restrains Proliferation of Receiving Cells

Cold shock proteins: from cellular mechanisms to pathophysiology and disease

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