The pleiotropic functions of the Y-box-binding protein, YB-1

Kimitoshi Kohno; Hiroto Izumi; Takeshi Uchiumi; Megumi Ashizuka; Michihiko Kuwano

doi:10.1002/bies.10300

The pleiotropic functions of the Y-box-binding protein, YB-1

Kimitoshi Kohno, Hiroto Izumi, Takeshi Uchiumi, Megumi Ashizuka, Michihiko Kuwano

Research output: Contribution to journal › Review article › peer-review

432 Citations (Scopus)

Abstract

The Y-box-binding protein (YB-1) represents the most evolutionary conserved nucleic-acid-binding protein currently known. YB-1 is a member of the cold-shock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YB-1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YB-1 and will then summarize the pleiotropic functions brought about via DNA-RNA transaction and protein-protein interactions. In addition, we will discuss the diverse range of potential physiological and pathological functions of YB-1.

Original language	English
Pages (from-to)	691-698
Number of pages	8
Journal	BioEssays
Volume	25
Issue number	7
DOIs	https://doi.org/10.1002/bies.10300
Publication status	Published - Jul 1 2003
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1002/bies.10300

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abstract = "The Y-box-binding protein (YB-1) represents the most evolutionary conserved nucleic-acid-binding protein currently known. YB-1 is a member of the cold-shock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YB-1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YB-1 and will then summarize the pleiotropic functions brought about via DNA-RNA transaction and protein-protein interactions. In addition, we will discuss the diverse range of potential physiological and pathological functions of YB-1.",

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T1 - The pleiotropic functions of the Y-box-binding protein, YB-1

AU - Kohno, Kimitoshi

AU - Izumi, Hiroto

AU - Uchiumi, Takeshi

AU - Ashizuka, Megumi

AU - Kuwano, Michihiko

PY - 2003/7/1

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N2 - The Y-box-binding protein (YB-1) represents the most evolutionary conserved nucleic-acid-binding protein currently known. YB-1 is a member of the cold-shock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YB-1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YB-1 and will then summarize the pleiotropic functions brought about via DNA-RNA transaction and protein-protein interactions. In addition, we will discuss the diverse range of potential physiological and pathological functions of YB-1.

AB - The Y-box-binding protein (YB-1) represents the most evolutionary conserved nucleic-acid-binding protein currently known. YB-1 is a member of the cold-shock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YB-1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YB-1 and will then summarize the pleiotropic functions brought about via DNA-RNA transaction and protein-protein interactions. In addition, we will discuss the diverse range of potential physiological and pathological functions of YB-1.

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The pleiotropic functions of the Y-box-binding protein, YB-1

Abstract

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