The acyl‐CoA‐binding protein Acb1 regulates mitochondria, lipid droplets, and cell proliferation

He, Jiajia; Liu, Ke; Zheng, Shaoyong; Wu, Yifan; Zhao, Chao; Yan, Shuaijie; Liu, Ling; Ruan, Ke; Ma, Xiaopeng; Fu, Chuanhai

doi:10.1002/1873-3468.14415

Cited by 6 publications

(1 citation statement)

References 34 publications

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“…MiD proteins are only found in metazoans, so it is unclear whether LCACA influences mitochondrial fission in non-metazoans. Interestingly, knocking out cytoplasmic acyl-CoA binding protein in Schizosaccharomyces pombe causes DRP1-dependent mitochondrial fission 41 , implying that increasing levels of free acyl-CoA induces mitochondrial fission. The proteins mediating this effect remain to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

Long-chain fatty acyl-coenzyme A activates the mitochondrial fission factors MiD49 and MiD51 by inducing their oligomerization

Liu,

Kage,

Sapp

et al. 2023

Preprint

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Mitochondrial fission occurs in many cellular processes, but the regulation of fission is poorly understood. We show that long-chain acyl coenzyme A (LCACA) activates two related mitochondrial fission proteins, MiD49 and MiD51, by inducing their oligomerization, activating their ability to stimulate DRP1 GTPase activity. The 1:1 stoichiometry of LCACA:MiD in the oligomer suggests interaction in the previously identified nucleotide-binding pocket, and a point mutation in this pocket reduces LCACA binding and LCACA-induced oligomerization for MiD51. In cells, this LCACA binding mutant does not assemble into puncta on mitochondria or rescue MiD49/51 knock-down effects on mitochondrial length and DRP1 recruitment. Furthermore, cellular treatment with the fatty acid analogue 2-bromopalmitate, which causes increased acyl-CoA, promotes mitochondrial fission in an MiD49/51-dependent manner. These results suggest that LCACA is an endogenous ligand for MiDs, inducing mitochondrial fission and providing a potential mechanism for fatty acid-induced mitochondrial fragmentation. Finally, MiD49 or MiD51 oligomers synergize with MFF, but not with actin filaments, in DRP1 activation, suggesting distinct pathways for DRP1 activation.

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Section: Discussionmentioning

confidence: 99%

Long-chain fatty acyl-coenzyme A activates the mitochondrial fission factors MiD49 and MiD51 by inducing their oligomerization

Liu,

Kage,

Sapp

et al. 2023

Preprint

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The acyl-CoA-binding protein VdAcb1 is essential for carbon starvation response and contributes to virulence in Verticillium dahliae

Zhuang,

Zhang,

Sun

et al. 2024

aBIOTECH

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In the face of carbon, nitrogen, and phosphorus starvation, microorganisms have evolved adaptive mechanisms to maintain growth. In a previous study, we identified a protein predicted to contain acyl-CoA-binding domains in the plant pathogenic fungus Verticillium dahliae. The predicted protein, designated VdAcb1, possesses an atypical signal peptide. However, the functions of this acyl-CoA-binding protein in V. dahliae are not clear. In this research, in vivo or in vitro assays confirmed that VdAcb1 is secreted extracellularly from V. dahliae, although it does not have the typical signal peptide. Furthermore, the unconventional secretion of VdAcb1 was dependent on VdGRASP, a member of the compartment for unconventional protein secretion (CUPS). The deletion mutant strain of VdAcb1 (ΔVdAcb1) exhibited significant sensitivity to carbon starvation. RNA-seq revealed that the expression of genes related to filamentous growth (MSB2 pathway) and sugar transport were regulated by VdAcb1 under conditions of carbon starvation. Yeast one-hybrid experiments further showed that the expression of VdAcb1 was positively regulated by the transcription factor VdMsn4. The ΔVdAcb1 strain showed significantly reduced virulence on Gossypium hirsutum and Nicotiana benthamiana. We hypothesize that under conditions of carbon starvation, the expression of VdAcb1 is activated by VdMsn4 and VdAcb1 is secreted into the extracellular space. In turn, this activates the downstream MAPK pathway to enhance filamentous growth and virulence of V. dahliae.

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A distinct Acyl-CoA binding protein (ACBP6) shapes tissue plasticity during nutrient adaptation in Drosophila

Li,

Karpac

2023

Nat Commun

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Nutrient availability is a major selective force in the evolution of metazoa, and thus plasticity in tissue function and morphology is shaped by adaptive responses to nutrient changes. Utilizing Drosophila, we reveal that distinct calibration of acyl-CoA metabolism, mediated by Acbp6 (Acyl-CoA binding-protein 6), is critical for nutrient-dependent tissue plasticity. Drosophila Acbp6, which arose by evolutionary duplication and binds acyl-CoA to tune acetyl-CoA metabolism, is required for intestinal resizing after nutrient deprivation through activating intestinal stem cell proliferation from quiescence. Disruption of acyl-CoA metabolism by Acbp6 attenuation drives aberrant ‘switching’ of metabolic networks in intestinal enterocytes during nutrient adaptation, impairing acetyl-CoA metabolism and acetylation amid intestinal resizing. We also identified STAT92e, whose function is influenced by acetyl-CoA levels, as a key regulator of acyl-CoA and nutrient-dependent changes in stem cell activation. These findings define a regulatory mechanism, shaped by acyl-CoA metabolism, that adjusts proliferative homeostasis to coordinately regulate tissue plasticity during nutrient adaptation.

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The acyl‐CoA‐binding protein Acb1 regulates mitochondria, lipid droplets, and cell proliferation

Cited by 6 publications

References 34 publications

Long-chain fatty acyl-coenzyme A activates the mitochondrial fission factors MiD49 and MiD51 by inducing their oligomerization

Long-chain fatty acyl-coenzyme A activates the mitochondrial fission factors MiD49 and MiD51 by inducing their oligomerization

The acyl-CoA-binding protein VdAcb1 is essential for carbon starvation response and contributes to virulence in Verticillium dahliae

A distinct Acyl-CoA binding protein (ACBP6) shapes tissue plasticity during nutrient adaptation in Drosophila

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