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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2020.1
- 수록면
- 181 - 190 (10page)
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Protein phosphatase 4 (PP4), one of serine/threonine phosphatases, is involved in many critical cellular pathways, including DNA damage response (DNA repair, cell cycle regulation, and apoptosis), tumorigenesis, cell migration, immune response, stem cell development, glucose metabolism, and diabetes. PP4 has been steadily studied over the past decade about wide spectrum of physiological activities in cells. Given the many vital functions in cells, PP4 has great potential to develop into the finding of key working mechanisms and effective treatments for related diseases such as cancer and diabetes. In this review, we provide an overview of the cellular and molecular mechanisms by which PP4 impacts and also discuss the functional significance of it in cell health.
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참고문헌 (100)
참고문헌 신청
Brautigan DL / 2013 / Protein Ser/Thr phosphatases--the ugly ducklings of cell signalling / FEBS J 280:324~345
Lillo C / 2014 / Protein phosphatases PP2A, PP4 and PP6 : mediators and regulators in development and responses to environmental cues / Plant Cell Environ 37:2631~2648
Lee DH / 2011 / What goes on must come off : phosphatases gate-crash the DNA damage response / Trends Biochem Sci 36:569~577
Brewis ND / 1993 / PPX, a novel protein serine/threonine phosphatase localized to centrosomes / EMBO J 12:987~996
Lee DH / 2010 / A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination / Nat Struct Mol Biol 17:365~372
Lillo C / 2014 / Protein phosphatases PP2A, PP4 and PP6 : mediators and regulators in development and responses to environmental cues / Plant Cell Environ 37:2631~2648
Lee DH / 2011 / What goes on must come off : phosphatases gate-crash the DNA damage response / Trends Biochem Sci 36:569~577
Brewis ND / 1993 / PPX, a novel protein serine/threonine phosphatase localized to centrosomes / EMBO J 12:987~996
Lee DH / 2010 / A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination / Nat Struct Mol Biol 17:365~372
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