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MOLECULAR AND CELLULAR BIOLOGY, Dec. 2002, p. 85148526 Vol. 22, No. 24 0270-7306/02/$04.00 0 DOI: 10.1128/MCB.22.24.85148526.2002
 

Summary: MOLECULAR AND CELLULAR BIOLOGY, Dec. 2002, p. 85148526 Vol. 22, No. 24
0270-7306/02/$04.00 0 DOI: 10.1128/MCB.22.24.85148526.2002
Copyright 2002, American Society for Microbiology. All Rights Reserved.
A Novel Heterodimerization Domain, CRM1, and 14-3-3 Control
Subcellular Localization of the MondoA-Mlx Heterocomplex
Alanna L. Eilers, Eleanor Sundwall, Monica Lin, April A. Sullivan, and Donald E. Ayer*
Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah,
Salt Lake City, Utah 84112-5550
Received 19 July 2002/Returned for modification 4 September 2002/Accepted 13 September 2002
Among members of the bHLHZip family of transcriptional regulators, MondoA and Mlx have the unique
property of cytoplasmic localization. We have proposed that MondoA-Mlx heterodimers accumulate in the
nucleus in response to extracellular cues. Our previous work implicated heterodimerization between MondoA
and Mlx and a conserved domain in the N terminus of MondoA as important determinants of MondoA-Mlx
subcellular localization. MondoA and Mlx share sequence similarity in their bHLHZip domains and C termini.
Here we show that for both MondoA and Mlx, this C-terminal domain has cytoplasmic localization activity that
is required by the protein monomers to accumulate in the cytoplasm. This C-terminal domain is also a novel
dimerization interface that functions independently of the leucine zipper to mediate heterotypic interactions
between MondoA and Mlx. Dimerization between MondoA and Mlx inactivates the cytoplasmic localization
activity of their C termini and is necessary for the heterocomplex to accumulate in the nucleus. MondoA-Mlx
heterodimers, while poised for nuclear entry, are retained in the cytoplasm by conserved domains in the N

  

Source: Ayer, Don - Huntsman Cancer Institute, University of Utah

 

Collections: Biology and Medicine