![]()
|
|
||||||||
J. Biol. Chem., Vol. 275, Issue 43, 33336-33345, October 27, 2000
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Molecular Genetics and Microbiology,
University of Medicine & Dentistry of New Jersey, Robert Wood
Johnson Medical School, Piscataway, New Jersey 08854
The K562 leukemia cell line is bipotential for
erythroid and megakaryoblastic differentiation. The phorbol ester
12-O-tetradecanoylphorbol-13-acetate (TPA) activates a
genetic program of gene expression in these cells leading to their
differentiation into megakaryoblasts, a platelet precursor. Thus, K562
cells offer a means to examine early changes in gene expression
necessary for megakaryoblastic commitment and differentiation. An
essential requirement for differentiation of many hematopoietic cell
types is the down-regulation of c-myc expression, because
its constitutive expression blocks differentiation. TPA-induced
differentiation of K562 cells causes rapid down-regulation of
c-myc expression, due in part to an mRNA decay rate
that is 4-fold faster compared with dividing cells. A cell-free
mRNA decay system reconstitutes TPA-induced destabilization of
c-myc mRNA, but it requires at least two components for
reconstitution. One component fractionates to the post-ribosomal
supernatant from either untreated or treated cells. This component is
sensitive to cycloheximide and micrococcal nuclease. The other
component is polysome-associated and is induced or activated by TPA.
Although in dividing cells c-myc mRNA decays via a
sequential pathway involving removal of the poly(A) tract followed by
degradation of the mRNA body, TPA activates a
deadenylation-independent pathway. The cell-free mRNA decay system
reconstitutes this alternate decay pathway as well.
Regulation of c-myc mRNA Decay in
Vitro by a Phorbol Ester-inducible, Ribosome-associated
Component in Differentiating Megakaryoblasts*
*
This work was supported by Grant CA52443 from the National
Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Molecular
Genetics and Microbiology, UMDNJ-Robert Wood Johnson Medical School,
675 Hoes Lane, Piscataway, NJ 08854. Tel.: 732-235-3473; Fax:
732-235-5223; E-mail: brewerga@umdnj.edu.
This article has been cited by other articles:
![]() |
D. Sparanese and C. H. Lee CRD-BP shields c-myc and MDR-1 RNA from endonucleolytic attack by a mammalian endoribonuclease Nucleic Acids Res., February 28, 2007; 35(4): 1209 - 1221. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Liao, M. Patel, Y. Hu, S. Charles, D. J. Herrick, and G. Brewer Targeted Knockdown of the RNA-binding Protein CRD-BP Promotes Cell Proliferation via an Insulin-like Growth Factor II-dependent Pathway in Human K562 Leukemia Cells J. Biol. Chem., November 19, 2004; 279(47): 48716 - 48724. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Tourriere, I.-e. Gallouzi, K. Chebli, J. P. Capony, J. Mouaikel, P. van der Geer, and J. Tazi RasGAP-Associated Endoribonuclease G3BP: Selective RNA Degradation and Phosphorylation-Dependent Localization Mol. Cell. Biol., November 15, 2001; 21(22): 7747 - 7760. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |