Erythroleukemic Differentiation

Marks, Paul A.; Rifkind, Richard A.

doi:10.1146/annurev.bi.47.070178.002223

Cited by 723 publications

(370 citation statements)

References 73 publications

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“…Murine erythroleukemia (MEL) cells are definitive pro-erythroblast erythroid cells that can be induced to terminally differentiate in culture by the addition of chemical inducers such as HMBA or DMSO [38]. EKLF mRNA and protein are expressed in actively growing MEL cells prior to terminal differentiation [8].…”

Section: The Eklf Nuclear/cytoplasmic Ratio Is Not Altered By a Variementioning

confidence: 99%

“…We next used MEL cells to attempt to alter the EKLF distribution by a variety of treatments. First we checked whether cytoplasmic EKLF could be redistributed to the nucleus of MEL cells during terminal differentiation when adult β-globin, a well-characterized activation target of EKLF, is induced [38]. Differentiation of MEL cells was induced with HMBA over 0-48 hours.…”

Section: The Eklf Nuclear/cytoplasmic Ratio Is Not Altered By a Variementioning

confidence: 99%

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Non-random subcellular distribution of variant EKLF in erythroid cells

Quadrini¹,

Gruzglin²,

Bieker³

2008

Experimental Cell Research

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EKLF protein plays a prominent role during erythroid development as a nuclear transcription factor. Not surprisingly, exogenous EKLF quickly localizes to the nucleus. However, using two different assays we have unexpectedly found that a substantial proportion of endogenous EKLF resides in the cytoplasm at steady state in all erythroid cells examined. While EKLF localization does not appear to change during either erythroid development or terminal differentiation, we find that the protein displays subtle yet distinct biochemical and functional differences depending on which subcellular compartment it is isolated from, with PEST sequences possibly playing a role in these differences. Localization is unaffected by inhibition of CRM1 activity and the two populations are not differentiated by stability. Heterokaryon assays demonstrate that EKLF is able to shuttle out of the nucleus although its nuclear re-entry is rapid. These studies suggest there is an unexplored role for EKLF in the cytoplasm that is separate from its well-characterized nuclear function.

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Section: The Eklf Nuclear/cytoplasmic Ratio Is Not Altered By a Variementioning

confidence: 99%

Section: The Eklf Nuclear/cytoplasmic Ratio Is Not Altered By a Variementioning

confidence: 99%

Non-random subcellular distribution of variant EKLF in erythroid cells

Quadrini¹,

Gruzglin²,

Bieker³

2008

Experimental Cell Research

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“…Friend virus-infected mouse erythroleukemia (MEL) cell lines provide an early erythroid precursor model system that can be induced to terminally differentiate with chemical agents such as HMBA in cell culture (Friend et al, 1971;Marks and Rifkind, 1978). Expression of c-Myb is downregulated during MEL cell differentiation, and forced expression of c-Myb blocks chemically induced MEL cell differentiation (McClinton et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

The carbonic anhydrase I locus contains a c-Myb target promoter and modulates differentiation of murine erythroleukemia cells

2006

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“…Expression of a variety of erythroid-speci®c genes including globin and glycophorin genes is induced in MEL cells in response to treatment with DMSO (Friend et al, 1971;Marks and Rifkind, 1978;Matsui et al, 1989). We previously identi®ed a locus control region (LCR)-like region (Gp-LCR) located far upstream of the mouse glycophorin gene (Terajima et al, 1994(Terajima et al, , 1995Nemoto et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

et al. 1998

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We previously reported that YY-1, a versatile transcription factor, regulates expression of glycophorin gene by binding to its locus control region-like region (Gp-LCR) in combination with E-box binding protein during murine erythroleukemia (MEL) cell di erentiation. In the present work, we demonstrated that YY-1 and c-Myc, a nuclear oncoprotein, were physically associated in vivo and that down regulation of c-Myc liberated free YY-1 from its complex, resulting in the functional binding of YY-1 to the Gp-LCR. We also showed that the E-box binding protein (EBP) which bound to E-box was physically associated with YY-1, facilitated binding of YY-1 to the neighboring site and their combinatorial binding may stimulate the GpLCR mediated enhancement of erythroid-speci®c transcription of glycophorin gene in MEL cells.

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Erythroleukemic Differentiation

Cited by 723 publications

References 73 publications

Non-random subcellular distribution of variant EKLF in erythroid cells

Non-random subcellular distribution of variant EKLF in erythroid cells

The carbonic anhydrase I locus contains a c-Myb target promoter and modulates differentiation of murine erythroleukemia cells

Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

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