The 14-3-3 proteins constitute a family of dimeric proteins that are involved in many cellular functions. At least two mammalian 14-3-3 proteins can form heterodimers and the approximate regions important for dimerization have been identified. in this study, we demonstrate that eight Arabidopsis and one maize 14-3-3 protein can dimerize with each other and with themselves. Native gel Western analysis of Arabidopsis cell extract also suggests the presence of 14-3-3 heterodimers in vivo. Finally, we identified the domains of one 14-3-3 protein that are sufficient for homodimerization and heterodimerization. These data support the hypothesis that evolutionarily divergent 14-3-3 proteins can interact with each other to form diverse molecular modulators or adapters in signaling pathways. (C) 1997 Academic Press.
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WASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USAWASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USA
FANTL, WJ
MUSLIN, AJ
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WASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USAWASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USA
MUSLIN, AJ
KIKUCHI, A
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WASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USAWASHINGTON UNIV, SCH MED, DIV BIOORGAN CHEM & MOLEC PHARMACOL, ST LOUIS, MO 63110 USA
KIKUCHI, A
MARTIN, JA
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MARTIN, JA
MACNICOL, AM
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MACNICOL, AM
GROSS, RW
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GROSS, RW
WILLIAMS, LT
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FANTL, WJ
MUSLIN, AJ
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KIKUCHI, A
MARTIN, JA
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MARTIN, JA
MACNICOL, AM
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MACNICOL, AM
GROSS, RW
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