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Blood, 1 January 2002, Vol. 99, No. 1, pp. 275-281
NEOPLASIA
The MLL fusion partner AF10 binds GAS41, a
protein that interacts with the human SWI/SNF complex
Silvana Debernardi,
Alessandra Bassini,
Louise K. Jones,
Tracy Chaplin,
Britta Linder,
Diederik R. H. de Bruijn,
Eckart Meese, and
Bryan D. Young
From the Imperial Cancer Research Fund, Department of
Medical Oncology, St Bartholomew's Hospital Medical College,
London, United Kingdom; Department of Human Genetics, University
Hospital Nijmegen, The Netherlands; and the Department of Human
Genetics, Medical School, University of Saar, Homburg/ Saar, Germany.
The AF10 gene encodes a putative transcription factor
containing an N-terminal LAP/PHD zinc finger motif, a functional
nuclear localization signal, an AT-hook domain, and a leucine zipper
toward the C-terminus. AF10 is involved in 2 distinct
chromosomal translocations associated with hematologic malignancy. The
chimeric fusion proteins MLL/AF10 and CALM/AF10, resulting from the
t(10;11)(p12;q23) and the t(10;11)(p12;q14), respectively, consistently
retain the leucine zipper motif of AF10. This part of the
C-terminal region was used as bait in a yeast 2 hybrid screening of a
testis complementary DNA library. The leucine zipper interacted with
GAS41, a protein previously identified as the product of an amplified
gene in a glioblastoma. GAS41 shows significant homology to the
Saccharomyces cerevisiae protein ANC1 and to the human MLL
fusion partners AF9 and ENL. The interaction was confirmed in vivo.
Furthermore, the study showed by coimmunoprecipitation that GAS41
interacts with INI1 (Integrase Interactor 1) and that INI1 was present
in the AF10 immunoprecipitate. INI1 is the human homologue of the yeast SNF5 protein, a component of the SWI/SNF complex, which acts to remodel
chromatin and to modulate transcription. The retention of the leucine
zipper in the MLL and CALM fusions suggests that a key feature of these
chimeric proteins may be their ability to interfere in normal
gene regulation through interaction with the adenosine
triphosphate-dependent chromatinremodeling complexes.
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