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XB-ART-5523
Nat Neurosci 2003 May 01;65:468-75. doi: 10.1038/nn1041.
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A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels.

Maeno-Hikichi Y , Chang S , Matsumura K , Lai M , Lin H , Nakagawa N , Kuroda S , Zhang JF .


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Multiple protein kinase C (PKC) isozymes are present in neurons, where they regulate a variety of cellular functions. Due to the lack of specific PKC isozyme inhibitors, it remains unknown how PKC acts on its selective target(s) and achieves its specific actions. Here we show that a PKC binding protein, enigma homolog (ENH), interacts specifically with both PKCepsilon and N-type Ca2+ channels, forming a PKCepsilon-ENH-Ca2+ channel macromolecular complex. Coexpression of ENH facilitated modulation of N-type Ca2+ channel activity by PKC. Disruption of the complex reduced the potentiation of the channel activity by PKC in neurons. 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.

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Species referenced: Xenopus laevis
Genes referenced: pdlim7 prkce

References :
Gardezi, PDLIM5 is not a neuronal CaV2.2 adaptor protein. 2009, Pubmed