Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation

Bersuker, Kirill; Olzmann, James A.

doi:10.1016/j.bbalip.2017.06.006

Cited by 127 publications

(131 citation statements)

References 155 publications

(232 reference statements)

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“…Another 3% of the proteome (five proteins) comprised proteins involved in protein degradation. LDs were found to play a role in the degradation of apolipoprotein B‐100 and HMG‐CoA reductase and proposed to be functionally involved in protein degradation . Six proteins involved in the signalling pathway comprised 3% of the total proteins, supporting the hypothesis that LDs are involved in signal transduction .…”

Section: Resultsmentioning

confidence: 83%

Comparative proteomic study of liver lipid droplets and mitochondria in mice housed at different temperatures

Zhou

Liu

et al. 2019

FEBS Letters

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Laboratory mice are standardly housed at around 23 °C, setting them under chronic cold stress. Metabolic changes in the liver in mice housed at thermoneutral, standard and cold temperatures remain unknown. In the present study, we isolated lipid droplets and mitochondria from their livers in a comparative proteomic study aiming to investigate the changes. According to proteomic analysis, mitochondrial tricarboxylic acid cycle (TCA cycle) and retinol metabolism are enhanced, whereas oxidative phosphorylation is not affected obviously under cold conditions, suggesting that liver mitochondria may increase TCA cycle capacity in biosynthetic pathways, as well as retinol metabolism, to help the liver to adapt. Based on proteomic and immunoblotting results, perilipin 5 and major urinary proteins are increased significantly, whereas mitochondrial pyruvate carrier is decreased dramatically under cold conditions, indicating their involvement in liver adaptation.

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Section: Resultsmentioning

confidence: 83%

Comparative proteomic study of liver lipid droplets and mitochondria in mice housed at different temperatures

Zhou

Liu

et al. 2019

FEBS Letters

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“…To investigate the possible mechanism by which LD‐associated proteins localize specifically to the organelle, the current known localization patterns of LD‐associated proteins and common structural features are listed in Table and Figure based on previous researches and reviews …”

Section: The Localization Patterns Of Lipid Droplet Proteinsmentioning

confidence: 99%

The New Face of the Lipid Droplet: Lipid Droplet Proteins

Zhang

Liu

2018

Proteomics

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The lipid droplet (LD) is an organelle with vital functions found in nearly all organisms. LD proteomic research has provided fundamentally important insights into this organelle's functions. The review provides a summary of LD proteomic studies conducted across diverse organisms and cell and tissue types. The accumulated proteomic data are reviewed for evidence of a protein targeting mechanism for the organelle. The hypotheses for several specific localization mechanisms based on what is known about targeting mechanisms for other organelles and vesicles are provided. Although the nature of the mechanism is not known, the functional data demonstrate that the targeting mechanism and, indeed, the organelle itself, is conserved from prokaryotes to eukaryotes. It is hoped that the review will help inspire further research leading to novel discoveries in the field.

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“…a-tubulin served as an endogenous control. the 1-106 polypeptide sequence for possible structural features including hydrophobic domains and amphipathic ahelices, which are known to serve as LD targeting signals in mammals and yeast (Kory et al, 2016;Bersuker and Olzmann, 2017). This analysis revealed a possible amphipathic a-helix ( Figure 3d) that corresponded to the moderately hydrophobic sequence present in the N-terminal region (residues 50-65, see Figure 3b).…”

Section: Ldip Is a Plant-specific Protein That Is Constitutively Exprmentioning

confidence: 99%

“…LDIP is class II-type LD coat protein LD proteins can target the LD surface either by binding the lipids of the phospholipid monolayer and/or neutral lipid core or by associating with other coat proteins (Kory et al, 2016;Bersuker and Olzmann, 2017). In general, they are divided into two classes: class I proteins, including the oleosins, which target to the LD surface via the ER , and class II proteins, which target directly from the cytoplasm.…”

Section: Identification Of Ldip As An Ld-localized Plant-specific Prmentioning

confidence: 99%

Arabidopsis lipid droplet‐associated protein (LDAP) – interacting protein (LDIP) influences lipid droplet size and neutral lipid homeostasis in both leaves and seeds

et al. 2017

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Cytoplasmic lipid droplets (LDs) are found in all types of plant cells; they are derived from the endoplasmic reticulum and function as a repository for neutral lipids, as well as serving in lipid remodelling and signalling. However, the mechanisms underlying the formation, steady-state maintenance and turnover of plant LDs, particularly in non-seed tissues, are relatively unknown. Previously, we showed that the LD-associated proteins (LDAPs) are a family of plant-specific, LD surface-associated coat proteins that are required for proper biogenesis of LDs and neutral lipid homeostasis in vegetative tissues. Here, we screened a yeast two-hybrid library using the Arabidopsis LDAP3 isoform as 'bait' in an effort to identify other novel LD protein constituents. One of the candidate LDAP3-interacting proteins was Arabidopsis At5g16550, which is a plant-specific protein of unknown function that we termed LDIP (LDAP-interacting protein). Using a combination of biochemical and cellular approaches, we show that LDIP targets specifically to the LD surface, contains a discrete amphipathic α-helical targeting sequence, and participates in both homotypic and heterotypic associations with itself and LDAP3, respectively. Analysis of LDIP T-DNA knockdown and knockout mutants showed a decrease in LD abundance and an increase in variability of LD size in leaves, with concomitant increases in total neutral lipid content. Similar phenotypes were observed in plant seeds, which showed enlarged LDs and increases in total amounts of seed oil. Collectively, these data identify LDIP as a new player in LD biology that modulates both LD size and cellular neutral lipid homeostasis in both leaves and seeds.

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Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation

Cited by 127 publications

References 155 publications

Comparative proteomic study of liver lipid droplets and mitochondria in mice housed at different temperatures

Comparative proteomic study of liver lipid droplets and mitochondria in mice housed at different temperatures

The New Face of the Lipid Droplet: Lipid Droplet Proteins

Arabidopsis lipid droplet‐associated protein (LDAP) – interacting protein (LDIP) influences lipid droplet size and neutral lipid homeostasis in both leaves and seeds

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