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. Author manuscript; available in PMC: 2018 Dec 1.
Published in final edited form as: Cell Signal. 2017 Aug 18;40:1–9. doi: 10.1016/j.cellsig.2017.08.005

Figure 1.

Figure 1

PKC structure is similar across family members, although they have different activation requirements. The inhibitory pseudosubstrate domain and the kinase domain, consisting of C3 and C4, are similar amongst PKCs, but the regulatory domains differ. Conventional PKCs (cPKCs) require DAG and calcium binding, while novel PKCs (nPKCs) require DAG binding, and atypical PKCs (aPKCs) require neither DAG nor calcium binding, although they have a single Cys-rich motif (C1).