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. 2020 May 5;295(27):8928–8944. doi: 10.1074/jbc.RA120.012624

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© 2020 Trcka et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 6. — Phosphorylation of Ser¹⁶⁰ modulates TOMM34 interaction with HSP70 protein. a, SBP pulldown analysis of the interaction between SBP–HSP70/SBP–HSP90 and nonphosphorylated (Non-phos) and PKA-phosphorylated (Phos) TOMM34 protein variants. Because the interaction of TOMM34 with HSP70 is ATP-dependent (21), these experiments were performed in the presence or absence of ATP. b, SBP pulldown analysis of SBP–HSP70/SBP–HSP90 interaction with nonphosphorylated and PKA-phosphorylated TOMM34 and/or S93A/S160A proteins in the presence and the absence of 14-3-3γ. C+ denotes purified 14-3-3γ protein used as a positive control for Western blotting.