Figure 1 | Scientific Reports

Figure 1

From: Analysis of the CaMKIIα and β splice-variant distribution among brain regions reveals isoform-specific differences in holoenzyme formation

Figure 1

Structure of CaMKII isoforms and splice-variants. (a) The CaMKII holoenzyme structure (upper panels) and protein domain sequence (lower panel). An N-terminal kinase domain (blue; encoded by 10 exons) is followed by the Ca2+/CaM-binding regulatory domain (green; encoded by two exons), the variable linker domain (orange; subject to alternative splicing), and the C-terminal hub domain (aqua; encoded by three exons) that mediates holoenzyme formation. (b) The exons encoding the variable domain of the four mammalian CaMKII isoforms in comparison. Exclusion of specific exons in specific splice variants of the α and β isoforms are indicated. Note that exons v2 and v6 (dark orange) appears to be included in almost all splice variants of all CaMKII isoforms; inclusion of exon v3N (red) generates a functional nuclear localization signal.

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