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Molecular Chaperone GRP94 Binds to the Fanconi Anemia Group C
Protein and Regulates Its Intracellular Expression
Taizo Hoshino,
Jianxiang Wang,
Marcel P. Devetten,
Nobuhisa Iwata,
Sachiko Kajigaya,
Robert J. Wise,
Johnson M. Liu, and
Hagop Youssoufian
From the Department of Molecular and Human Genetics, Baylor College
of Medicine, Houston, TX; the Hematology Branch, National Heart, Lung
and Blood Institute, Bethesda, MD; and the Hematology-Oncology
Division, Brigham and Women's Hospital, Boston, MA.
The FAC protein encoded by the gene defective in Fanconi anemia (FA)
complementation group C binds to at least three ubiquitous cytoplasmic
proteins in vitro. We used here the complete coding sequence of
FAC in a yeast two-hybrid screen to identify interacting proteins. The molecular chaperone GRP94 was isolated twice from a
B-lymphocyte cDNA library. Binding was confirmed by
coimmunoprecipitation of FAC and GRP94 from cytosolic, but not nuclear,
lysates of transfected COS-1 cells, as well as from mouse liver
cytoplasmic extracts. Deletion mutants of FAC showed that residues
103-308 were required for interaction with GRP94, and a natural
splicing mutation within the IVS-4 of FAC that removes residues 111-148 failed to bind GRP94. Ribozyme-mediated inactivation of GRP94 in the
rat NRK cell line led to significantly reduced levels of immunoreactive FAC and concomitant hypersensitivity to mitomycin C, similar to the
cellular phenotype of FA. Our results demonstrate that GRP94 interacts
with FAC both in vitro and in vivo and regulates its intracellular
level in a cell culture model. In addition, the pathogenicity of the
IVS-4 splicing mutation in the FAC gene may be mediated in part
by its inability to bind to GRP94.
Blood, Vol. 91 No. 11 (June 1), 1998:
pp. 4379-4386
© 1998 by The American Society of Hematology.
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