PubMed_ArguminSci  

PubMed:16407284 JSONTXT 21 Projects

Annnotations TAB TSV DIC JSON TextAE-old TextAE

Id Subject Object Predicate Lexical cue
T1 68-178 DRI_Approach denotes Activation of NFAT transcription factors requires their dephosphorylation by the phosphatase calcineurin (CN).
T2 179-261 DRI_Approach denotes NFATs contain two CN binding motifs: PxIxIT and CnBP-B/CNBR2 (which we call LxVP).
T3 262-399 DRI_Approach denotes Here we carry out a detailed comparative analysis of the CN binding activity displayed by the PxIxIT and LxVP sites from different NFATs.
T4 400-554 DRI_Outcome denotes Dose-response CN binding experiments with GST fusion proteins of NFATc1 and NFATc2 showed that NFATc1 binds CN in vitro more efficiently than does NFATc2.
T5 555-809 DRI_Challenge denotes This difference in binding appears to be caused by the different CN binding potencies of the corresponding LxVP sites; thus while the LxVPc2 peptide fused to GST did not bind CN, GST-LxVPc1 bound it more efficiently than did GST-PxIxITc1 or GST-PxIxITc2.
T6 810-951 DRI_Outcome denotes Furthermore, an NFATc2 chimera protein containing the LxVP motif from NFATc1 interacted with CN much more potently than did wild-type NFATc2.
T7 952-1098 DRI_Outcome denotes Free peptides spanning the LxVP motifs from NFATc1, c3 or c4 displaced CN from GST-NFATc1 and GST-NFATc2 more efficiently than any PxIxIT peptide.
T8 1099-1145 DRI_Background denotes PxIxITc2 and LxVPc1 peptides were each able to
T9 1174-1202 DRI_Background denotes and GST-PxIxITc2-CN binding.
T10 1203-1332 DRI_Outcome denotes In contrast with PxIxITc2, the LxVP peptide not only blocked CN-NFAT binding but also inhibited CN phosphatase activity in vitro.
T11 1333-1428 DRI_Background denotes Furthermore, exogenous LxVPc1 blocked NFATc2 phosphorylation and nuclear translocation in vivo.
T12 1429-1641 DRI_Background denotes These results suggest a model in which the different CN binding characteristics of the PxIxIT and LxVP sites enable different NFAT members to influence each others activities in cells where they are co-expressed.