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. Author manuscript; available in PMC: 2010 Jul 8.
Published in final edited form as: Physiol Rev. 2008 Oct;88(4):1341–1378. doi: 10.1152/physrev.00034.2007

TABLE 1.

Structural basis for PKC isoform-RACK protein interactions

PKC Rack Protein ψRack Sequence Rack Binding Site
C2 domain V5 domain
PKCβ RACK1
SIKIWD		 241SVEIWD246 186MDPNGLSDPYVKL198
209KQKTKTIK216
218SLNPEWNET226 		βI graphic file with name nihms214620t1.jpg 621ACGRNAE627
645QEVIRN650
660SFVNSEFLKPEVKS673
PKCδ Annexin V
157VVLIQANRDPDAG164 		71IVLMRRAEDPMSE83 8SFNSYELGSL17 βII 645KLFIMN650
PKCε p32/gC1qBP
RACK2 or β′COP
285NNVALGYD292 		85HDAPIGYD92 14EAVSLKPT21

Sequences in RACK1, annexin V, p32/gC1qBP, and RACK2 that bind their respective PKC isoforms, PKC-ψ RACK sequences (that are homologous to the sequences on RACK proteins that bind PKC), and RACK binding sites on PKCβ, PKCδ, and PKCε are provided. Charged residues that underlie RACK-ψ RACK interactions are in bold.