| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| We studied the role of the interaction of calcineurin homologous protein 1 ( CHP 1 ) with the Na ( + ) / H ( + ) exchanger 1 ( NHE 1 ) , particularly its EF hand Ca ( 2+ ) binding motifs , in the intracellular pH ( pH ( 1 ) ) dependent regulation of NHE 1 . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP 2 bound to the cytoplasmic region of the Na+ / H+ exchanger NHE 1 . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| Like NHE 1 , CHP is widely expressed in human tissues . ^^^ Transient overexpression of CHP inhibits serum and GTP ase stimulated NHE 1 activity . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| CHP 2 , like CHP 1 , conferred the ability to NHEs 1 3 to express a high exchange activity by binding to the juxtamembrane region of the cytoplasmic domain of the exchanger , but it interacts more strongly ( approximately 5 fold ) with NHE 1 than does CHP 1 . ^^^ We produced stable cell clones overexpressing either CHP 1 or CHP 2 in which one of them is predominantly bound to NHE 1 . ^^^ Serum ( 10 % ) induced a significant cytoplasmic alkalinization ( 0 . 1 0 . 2 pH unit ) in cells co expressing CHP 1 and NHE 1 but not in cells co expressing CHP 2 and NHE 1 . ^^^ We propose that serum independent activation of NHE 1 by bound CHP 2 is one of the key mechanisms for the maintenance of high pH ( 1 ) and the resistance to serum deprivation induced cell death in malignantly transformed cells . . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| Crystal structure of CHP 2 complexed with NHE 1 cytosolic region and an implication for pH regulation . ^^^ Here , we report the first crystal structure of CHP ( CHP 2 isoform ) in complex with its binding domain in NHE 1 . ^^^ We show that the cytoplasmic alpha helix of NHE 1 is inserted into the hydrophobic cleft formed by N and C lobes of CHP 2 and that the size and shape of this crevice together with hydrogen bond formation at multiple positions assure a high degree of specificity for interaction with NHE members . ^^^ Structure based mutagenesis revealed the importance of hydrophobic interactions between CHP / NHE1 for the function of NHE 1 . ^^^ Furthermore , the crystal structure shows the existence of a protruding CHP unique region , and deletion of this region in CHP 2 inhibited the NHE 1 activity by inducing the acidic shift of intracellular pH dependence , while preserving interaction with NHE 1 . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| Ubiquitous calcineurin B homologous protein ( CHP or p 22 ) is co localized and co immunoprecipitated with expressed NHE 1 , NHE 2 , or NHE 3 independently of its myristoylation and Ca2+ binding , and its binding site was identified as the juxtamembrane region within the carboxyl terminal cytoplasmic domain of exchangers . ^^^ CHP binding defective mutations of NHE 1 3 or CHP depletion by injection of the competitive CHP binding region of NHE 1 into Xenopus oocytes resulted in a dramatic reduction ( > 90 % ) in the Na+ / H+ exchange activity . ^^^ |
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| Interacting proteins: Q99653 and P19634 |
Pubmed |
SVM Score :0.0 |
| NA |
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