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Papers In Press, published online ahead of print March 19, 2002
Division of Hematology-Oncology, Vanderbilt University Medical Center, Nashville, TN 37232
Corresponding Author: stephen.brandt{at}mcmail.vanderbilt.edu
The basic helix-loop-helix transcription factor TAL1 (or SCL), originally identified from its involvement by a chromosomal rearrangement in T-cell acute lymphoblastic leukemia, is required for hematopoietic development. TAL1 also has a critical role in embryonic vascular remodeling and is expressed in endothelial cells postnatally, although little is known about its function or regulation in this cell type. We report here that the important proangiogenic stimulus hypoxia stimulates phosphorylation, ubiquitination, and proteasomal breakdown of TAL1 in endothelial cells. Tryptic phosphopeptide mapping and chemical inhibitor studies showed that hypoxia induced the mitogen-activated protein kinase-mediated phosphorylation of a single serine residue, Ser122, in the protein, and site-directed mutagenesis demonstrated that Ser122 phosphorylation was necessary for hypoxic acceleration of TAL1 turnover in an immortalized murine endothelial cell line. Finally, while TAL1 expression was detected in endothelial cells from both large and small vessels, hypoxia-induced TAL1 turnover was observed only in microvascular endothelial cells. Besides their implications for TAL1 function in angiogenic processes, these results demonstrate that a protein kinase(s) important for mitogenic signalling is also utilized in hypoxic endothelial cells to target a transcription factor for destruction.
J. Biol. Chem, 10.1074/jbc.M109812200
Submitted on October 10, 2001
Revised on February 26, 2002
Accepted on March 19, 2002
Phosphorylation by mitogen-activated protein kinase mediates the hypoxia-induced turnover of the TAL1/SCL transcription factor in endothelial cells
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