Regulation of differentiation by a PHD domain in the NUP98-PHF23 fusion protein

Jocelyn C. Reader, Qixin Leng, Feyruz V. Rassool, Yi Ning

Research output: Contribution to journalArticle

Abstract

Acute myeloid leukemia (AML) is frequently associated with chromosomal translocations. These translocations produce specific fusion genes that play crucial roles in leukemogenesis. We recently identified a novel NUP98-PHF23 fusion in AML. In this study, we attempt to determine the role of NUP98-PHF23 protein and its plant homeodomain (PHD) and coiled-coil domain in regulation of cellular differentiation and protein distribution. We provide evidence that NUP98-PHF23, through its PHD domain, impairs TPA-induced differentiation of K562 cells. While the fusion protein localizes to the nucleus, its deletion mutant without the PHD domain resides exclusively in the nucleolus, suggesting a potential link between chromatin-binding PHD domain and nuclear architecture.

Original languageEnglish (US)
Pages (from-to)1094-1097
Number of pages4
JournalLeukemia Research
Volume34
Issue number8
DOIs
StatePublished - Aug 2010
Externally publishedYes

Fingerprint

Acute Myeloid Leukemia
Plant Proteins
Genetic Translocation
Proteins
K562 Cells
Gene Fusion
Chromatin
nuclear pore complex protein 98

Keywords

  • Differentiation
  • NUP98-PHF23 fusion
  • PHD domain

ASJC Scopus subject areas

  • Cancer Research
  • Hematology
  • Oncology

Cite this

Regulation of differentiation by a PHD domain in the NUP98-PHF23 fusion protein. / Reader, Jocelyn C.; Leng, Qixin; Rassool, Feyruz V.; Ning, Yi.

In: Leukemia Research, Vol. 34, No. 8, 08.2010, p. 1094-1097.

Research output: Contribution to journalArticle

Reader, Jocelyn C. ; Leng, Qixin ; Rassool, Feyruz V. ; Ning, Yi. / Regulation of differentiation by a PHD domain in the NUP98-PHF23 fusion protein. In: Leukemia Research. 2010 ; Vol. 34, No. 8. pp. 1094-1097.
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