Abstract：
: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.
journal_name
Nat Neuroscijournal_title
Nature neuroscienceauthors
Maeno-Hikichi Y,Chang S,Matsumura K,Lai M,Lin H,Nakagawa N,Kuroda S,Zhang JFdoi
10.1038/nn1041subject
Has Abstractpub_date
2003-05-01 00:00:00pages
468-75issue
5eissn
1097-6256issn
1546-1726pii
nn1041journal_volume
6pub_type
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