Title: Identification of a new calcineurin‐binding region in nuclear factor of activated T cells
Abstract:Calcineurin (CN), a Ca2+/calmodulin-dependent protein phosphatase, plays an important role in immunological and other biological functions. CN dephosphorylates nuclear factor of activated T cells (NFA...Calcineurin (CN), a Ca2+/calmodulin-dependent protein phosphatase, plays an important role in immunological and other biological functions. CN dephosphorylates nuclear factor of activated T cells (NFAT), which regulates transcription of numerous genes in T cells and other cell types/tissues. Two CN-binding regions have been identified in N- (CNBR1) and C- (CNBR2) terminuses of Ca2+-regulatory domain (CRD) of NFAT. This study was performed to elucidate the relative contribution of known and unknown CNBRs to CN/NFAT-binding. CN-binding activity with recombinant GST-fusion proteins of whole and partial domains of NFAT-CRD was measured by semi-quantitative immunoprecipitation assay. Besides CNBR1 and CNBR2, the region between CNBR1 and CNBR2 (CNBR3) was newly identified as a CN-binding domain of NFAT. CN-binding activity of CNBR3 was equivalent to that of CNBR1 and CNBR2. In comparison among NFAT subtypes, the potency of CN-binding activity of CNBR3 was NFAT2=NFAT3>NFAT4=NFAT1. Further mapping studies demonstrated that the critical CN-binding region of NFAT-CNBR3 potentially exists in and around its conserved Ser-Pro repeat-associated motif. Our present findings are useful to develop a novel means to regulate CN/NFAT-dependent biological reactions.Read More
Publication Year: 2006
Publication Date: 2006-03-01
Language: en
Type: article
Indexed In: ['crossref']
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Title: $Identification of a new calcineurin‐binding region in nuclear factor of activated T cells
Abstract: Calcineurin (CN), a Ca2+/calmodulin-dependent protein phosphatase, plays an important role in immunological and other biological functions. CN dephosphorylates nuclear factor of activated T cells (NFAT), which regulates transcription of numerous genes in T cells and other cell types/tissues. Two CN-binding regions have been identified in N- (CNBR1) and C- (CNBR2) terminuses of Ca2+-regulatory domain (CRD) of NFAT. This study was performed to elucidate the relative contribution of known and unknown CNBRs to CN/NFAT-binding. CN-binding activity with recombinant GST-fusion proteins of whole and partial domains of NFAT-CRD was measured by semi-quantitative immunoprecipitation assay. Besides CNBR1 and CNBR2, the region between CNBR1 and CNBR2 (CNBR3) was newly identified as a CN-binding domain of NFAT. CN-binding activity of CNBR3 was equivalent to that of CNBR1 and CNBR2. In comparison among NFAT subtypes, the potency of CN-binding activity of CNBR3 was NFAT2=NFAT3>NFAT4=NFAT1. Further mapping studies demonstrated that the critical CN-binding region of NFAT-CNBR3 potentially exists in and around its conserved Ser-Pro repeat-associated motif. Our present findings are useful to develop a novel means to regulate CN/NFAT-dependent biological reactions.