Monoubiquitination of Ancient Ubiquitous Protein 1 Promotes Lipid Droplet Clustering

Lohmann, Daniel; Spandl, Johanna; Stevanović, Ana; Schoene, Mario; Philippou‐Massier, Julia; Thiele, Christoph

doi:10.1371/journal.pone.0072453

Cited by 30 publications

(27 citation statements)

References 64 publications

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“…LDs tend to cluster together under certain conditions or when specific proteins are over-expressed [35][36][37][38][39]. However, for the most part these observations of changes in LD proximity do not conclusively document direct contact sites between adjacent LDs.…”

Section: Ld-ld Contact Sitesmentioning

confidence: 91%

Lipid droplet–organelle interactions: emerging roles in lipid metabolism

Barbosa

Savage

Siniossoglou

2015

Current Opinion in Cell Biology

140

106

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Cellular homeostasis depends on the precisely coordinated use of lipids as fuels for energy production, building blocks for membrane biogenesis or chemical signals for intra-cellular and inter-cellular communication. Lipid droplets (LDs) are universally conserved dynamic organelles that can store and mobilize fatty acids and other lipid species for their multiple cellular roles. Increasing evidence suggests that contact zones between LDs and other organelles play important roles in the trafficking of lipids and in the regulation of lipid metabolism. Here we review recent advances regarding the nature and functional relevance of interactions between LDs and other organelles-particularly the endoplasmic reticulum (ER), LDs, mitochondria and vacuoles-that highlight their importance for lipid metabolism.

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Section: Ld-ld Contact Sitesmentioning

confidence: 91%

Lipid droplet–organelle interactions: emerging roles in lipid metabolism

Barbosa

Savage

Siniossoglou

2015

Current Opinion in Cell Biology

140

106

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“…Ubiquitin can mediate interactions with proteins containing ubiquitin-binding domains (e.g. CUE, UBA, and UIM domains), such as AUP1, which contains a CUE domain [87,136]. AUP1 was also found to be monoubiquitinated and diubiquitinated (or monoubiquitinated on multiple lysines) [87,136].…”

Section: Connections Between Lds and The Ubiquitin-proteasome Systemmentioning

confidence: 99%

“…CUE, UBA, and UIM domains), such as AUP1, which contains a CUE domain [87,136]. AUP1 was also found to be monoubiquitinated and diubiquitinated (or monoubiquitinated on multiple lysines) [87,136]. Interestingly, overexpression of AUP1 was sufficient to induce LD clustering [136].…”

Section: Connections Between Lds and The Ubiquitin-proteasome Systemmentioning

confidence: 99%

“…AUP1 was also found to be monoubiquitinated and diubiquitinated (or monoubiquitinated on multiple lysines) [87,136]. Interestingly, overexpression of AUP1 was sufficient to induce LD clustering [136]. The clustering phenotype was dependent on the ubiquitination status of AUP1, since overexpression of a CUE domain mutant that was not ubiquitinated did not induce clustering, but fusion of this mutant to ubiquitin at its C-terminus rescued AUP1-induced clustering [136].…”

Section: Connections Between Lds and The Ubiquitin-proteasome Systemmentioning

confidence: 99%

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

Bersuker

Olzmann

2017

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

123

118

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Lipid droplets (LDs) are ubiquitous, endoplasmic reticulum (ER)-derived organelles that mediate the sequestration of neutral lipids (e.g. triacylglycerol and sterol esters), providing a dynamic cellular storage depot for rapid lipid mobilization in response to increased cellular demands. LDs have a unique ultrastructure, consisting of a core of neutral lipids encircled by a phospholipid monolayer that is decorated with integral and peripheral proteins. The LD proteome contains numerous lipid metabolic enzymes, regulatory scaffold proteins, proteins involved in LD clustering and fusion, and other proteins of unknown function. The function of LDs is inherently determined by the composition of its proteome and alteration of the LD protein coat provides a powerful mechanism to adapt LDs to fluctuating metabolic states. Here, we review the current understanding of the molecular mechanisms that govern LD protein targeting and degradation.

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“…Similar coalescence of lipid droplets was observed in BY-2 cells transiently overexpressing Arabidopsis LDaP (Gidda SK, Watt SC, and mullen rt, unpublished), as well as in various other cells types in which other lipid droplet proteins, such as perilipin 1 and the ancient ubiquitous protein 1, are ectopically (over)expressed. 20,21 Shown also is the corresponding differential interference contrast (DiC) image. Bar = 10 μm.…”

Section: Figure 2 Expression Pattern Of Ldaps In Oil Palm (E Guineementioning

confidence: 99%

Lipid droplet-associated proteins (LDAPs) are involved in the compartmentalization of lipophilic compounds in plant cells

Gidda

Watt²,

Collins-Silva

et al. 2013

Plant Signaling & Behavior

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Lipid droplets play an essential role in the life cycle of plants by housing lipid storage compounds, usually triacylglycerols, in seeds that are mobilized to support post-germinative growth, prior to photosynthetic establishment. Given this critical role in plant growth and development, the majority of research on plant lipid droplets has focused on their function in seed tissues. For instance, purification of lipid droplets from plant oilseeds resulted in the identification and characterization of the oleosins, which are an abundant class of lipid droplet-surface-associated proteins important for stabilizing lipid droplets during seed desiccation 1-3 and possibly serving as sites for recruitment of lipases that facilitate the breakdown of stored triacylglycerols during seedling establishment. 4 It is now appreciated, however, that lipid droplets have numerous functions beyond lipid storage in seeds and that they are present in nearly all plant cell types, many of which do not accumulate appreciable amounts of lipid, such as the cells in leaves, stems, and roots.5 There is also emerging evidence that lipid droplets are highly dynamic organelles involved in a variety of cellular processes and physiological responses, some of which appear to be conserved among eukaryotes. [6][7][8] Nevertheless, the precise functions of lipid droplets in non-seed cell types in plants are currently poorly understood.In an effort to increase our understanding of lipid droplet biogenesis and functions in plants, we recently characterized the proteome of lipid droplets isolated from the mesocarp of avocado (Persea americana).9 This tissue was selected for analysis since it is a rich source of non-seed lipid droplets that lack the abundant oleosins found in oilseed tissues. Briefly, proteins enriched in the isolated avocado mesocarp lipid droplet fraction were identified using a combination of multi-dimensional protein identification technology and peptide mass fingerprinting, using an avocado RNAseqderived "proteome" for query. Two of the most abundant proteins associated with these lipid droplets were highly similar (86%) in sequence to each other and, thus, were annotated as lipid dropletassociated protein 1 (LDAP1) and LDAP2 ( Fig. 1A; Pam_LDAP1 and Pam_LDAP2). We also showed previously that LDAP1 and LDAP2 gene expression during development of avocado mesocarp increased in correlation with oil accumulation.9 Interestingly, transcriptome analysis of various tissues of oil palm (Elaeis guineensis) revealed the presence of three LDAP-like genes, of which one of While lipid droplets have traditionally been considered as inert sites for the storage of triacylglycerols and sterol esters, they are now recognized as dynamic and functionally diverse organelles involved in energy homeostasis, lipid signaling, and stress responses. unlike most other organelles, lipid droplets are delineated by a half-unit membrane whose protein constituents are poorly understood, except in the specialized case of oleosins, which are associated with seed li...

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Monoubiquitination of Ancient Ubiquitous Protein 1 Promotes Lipid Droplet Clustering

Cited by 30 publications

References 64 publications

Lipid droplet–organelle interactions: emerging roles in lipid metabolism

Lipid droplet–organelle interactions: emerging roles in lipid metabolism

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

Lipid droplet-associated proteins (LDAPs) are involved in the compartmentalization of lipophilic compounds in plant cells

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