| Interacting proteins: Q96HC4 and Q02156 |
Pubmed |
SVM Score :0.95387568 |
| Thus , ENH , by interacting specifically with both PKCepsilon and the N type Ca2+ channel , targets a specific PKC to its substrate to form a functional signaling complex , which is the molecular mechanism for the specificity and efficiency of PKC signaling . . 0.95387568^^^ |
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| Interacting proteins: Q96HC4 and Q02156 |
Pubmed |
SVM Score :0.0 |
| Essential role of the LIM domain in the formation of the PKCepsilon ENH N type Ca2+ channel complex . ^^^ In a recent study , we have demonstrated that ENH , which has three consecutive LIM domains , acts as an adaptor protein for the formation of a functional PKCepsilon ENH N type Ca2+ channel complex in neurons . ^^^ Within the physiological Ca2+ concentration range ( 0 300 microM ) , binding of ENH to the channel C terminus was significantly increased by Ca2+ , whereas increased Ca2+ levels led to dissociation of PKCepsilon from ENH . ^^^ Mutagenesis studies revealed that the second LIM domain in ENH was primarily responsible for Ca2+ dependent binding of ENH to both the Ca2+ channel C terminus and PKCepsilon . ^^^ PKCepsilon translocation inhibition peptide , which blocks the translocation of PKCepsilon from the cytosol to the membrane , inhibited the interaction between PKCepsilon and ENH . ^^^ |
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