TY - JOUR
T1 - Zeta inhibitory peptide disrupts electrostatic interactions that maintain atypical protein Kinase C in its active conformation on the scaffold p62
AU - Tsai, Li Chun Lisa
AU - Xie, Lei
AU - Dore, Kim
AU - Xie, Li
AU - Del Rio, Jason C.
AU - King, Charles C.
AU - Martinez-Ariza, Guillermo
AU - Hulme, Christopher
AU - Malinow, Roberto
AU - Bourne, Philip E.
AU - Newton, Alexandra C.
PY - 2015/9/4
Y1 - 2015/9/4
N2 - Background: How atypical PKCs are maintained in an active conformation is unknown. Results: We identify an acidic surface on the aPKC scaffold, p62, that tethers the kinase's autoinhibitory pseudosubstrate to allow activity. The biologically active basic peptide, ZIP, competes for binding to this surface, resulting in localized aPKC autoinhibition. Conclusion: P62 tethers aPKCs in an active conformation. Significance: P62 is a molecular target for ZIP.
AB - Background: How atypical PKCs are maintained in an active conformation is unknown. Results: We identify an acidic surface on the aPKC scaffold, p62, that tethers the kinase's autoinhibitory pseudosubstrate to allow activity. The biologically active basic peptide, ZIP, competes for binding to this surface, resulting in localized aPKC autoinhibition. Conclusion: P62 tethers aPKCs in an active conformation. Significance: P62 is a molecular target for ZIP.
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U2 - 10.1074/jbc.M115.676221
DO - 10.1074/jbc.M115.676221
M3 - Article
C2 - 26187466
AN - SCOPUS:84941343009
SN - 0021-9258
VL - 290
SP - 21845
EP - 21856
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -