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Active and dynamic mitochondrial S-depalmitoylation revealed by targeted fluorescent probes.

Abstract：

:The reversible modification of cysteine residues by thioester formation with palmitate (S-palmitoylation) is an abundant lipid post-translational modification (PTM) in mammalian systems. S-palmitoylation has been observed on mitochondrial proteins, providing an intriguing potential connection between metabolic lipids and mitochondrial regulation. However, it is unknown whether and/or how mitochondrial S-palmitoylation is regulated. Here we report the development of mitoDPPs, targeted fluorescent probes that measure the activity levels of "erasers" of S-palmitoylation, acyl-protein thioesterases (APTs), within mitochondria of live cells. Using mitoDPPs, we discover active S-depalmitoylation in mitochondria, in part mediated by APT1, an S-depalmitoylase previously thought to reside in the cytosol and on the Golgi apparatus. We also find that perturbation of long-chain acyl-CoA cytoplasm and mitochondrial regulatory proteins, respectively, results in selective responses from cytosolic and mitochondrial S-depalmitoylases. Altogether, this work reveals that mitochondrial S-palmitoylation is actively regulated by "eraser" enzymes that respond to alterations in mitochondrial lipid homeostasis.

journal_name

Nat Commun

journal_title

Nature communications

authors

Kathayat RS,Cao Y,Elvira PD,Sandoz PA,Zaballa ME,Springer MZ,Drake LE,Macleod KF,van der Goot FG,Dickinson BC

doi

10.1038/s41467-017-02655-1

subject

Has Abstract

pub_date

2018-01-23 00:00:00

pages

334

issue

1

issn

2041-1723

pii

10.1038/s41467-017-02655-1

journal_volume

9

pub_type

杂志文章

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