Abstract:
:We previously demonstrated that beta II protein kinase C (βIIPKC) activity is elevated in failing hearts and contributes to this pathology. Here we report that βIIPKC accumulates on the mitochondrial outer membrane and phosphorylates mitofusin 1 (Mfn1) at serine 86. Mfn1 phosphorylation results in partial loss of its GTPase activity and in a buildup of fragmented and dysfunctional mitochondria in heart failure. βIIPKC siRNA or a βIIPKC inhibitor mitigates mitochondrial fragmentation and cell death. We confirm that Mfn1-βIIPKC interaction alone is critical in inhibiting mitochondrial function and cardiac myocyte viability using SAMβA, a rationally-designed peptide that selectively antagonizes Mfn1-βIIPKC association. SAMβA treatment protects cultured neonatal and adult cardiac myocytes, but not Mfn1 knockout cells, from stress-induced death. Importantly, SAMβA treatment re-establishes mitochondrial morphology and function and improves cardiac contractility in rats with heart failure, suggesting that SAMβA may be a potential treatment for patients with heart failure.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Ferreira JCB,Campos JC,Qvit N,Qi X,Bozi LHM,Bechara LRG,Lima VM,Queliconi BB,Disatnik MH,Dourado PMM,Kowaltowski AJ,Mochly-Rosen Ddoi
10.1038/s41467-018-08276-6subject
Has Abstractpub_date
2019-01-18 00:00:00pages
329issue
1issn
2041-1723pii
10.1038/s41467-018-08276-6journal_volume
10pub_type
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