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Label free comparative proteome analysis of Arabidopsis lipid droplets from 6 week old leaves

ABSTRACT: Lipid droplets from 6 week old Arabidopsis leaves were purified on sucrose gradient. The abundance of the proteins in the lipid droplet fraction was established by label free and compared to soluble, membrane and plastoglobule fractions, and total leaf extract in order to identify the proteins specifically enriched in lipid droplets. Three independent biological replicates, from three independent cultures were performed. For each biological replicates, three preparations of lipid droplets (and other fractions) within each of the three independent cultures were obtained.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Stephane Claverol

LAB HEAD: Claire Brehelin

PROVIDER: PXD006113 | Pride | 2017-06-19

REPOSITORIES: Pride

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			Action	DRS
	cb140521_02b.RAW	Raw
	cb140521_02b.msf	Msf
	cb140521_03b.RAW	Raw
	cb140521_03b.msf	Msf
	cb140521_03c.RAW	Raw

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Publications

Proteomic Analysis of Lipid Droplets from Arabidopsis Aging Leaves Brings New Insight into Their Biogenesis and Functions.

Brocard Lysiane L Immel Françoise F Coulon Denis D Esnay Nicolas N Tuphile Karine K Pascal Stéphanie S Claverol Stéphane S Fouillen Laëtitia L Bessoule Jean-Jacques JJ Bréhélin Claire C

Frontiers in plant science 20170529

Lipid droplets (LDs) are cell compartments specialized for oil storage. Although their role and biogenesis are relatively well documented in seeds, little is known about their composition, structure and function in senescing leaves where they also accumulate. Here, we used a label free quantitative mass spectrometry approach to define the LD proteome of aging Arabidopsis leaves. We found that its composition is highly different from that of seed/cotyledon and identified 28 proteins including 9 e ...[more]

PMID: 28611809

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Mass spectrometry-based proteomic characterization of lipid droplets from WT and abhd1 KO mutants of Chlamydomonas reinhardtii

Project description:Lipid droplets (LDs) are ubiquitous organelles and the major sites of fatty acid storage and energy homeostasis in eukaryotic cells. However, despite their physiological importance, few proteins involved in the mechanism of LD formation have been identified. Here, using the model microalga Chlamydomonas reinhardtii, we show that ABHD1, a member of the α/β hydrolase domain-containing protein family, is a novel type of LD-associated protein which stimulates LD formation through two distinct actions on the LD hemi-membrane, one enzymatic and the other structural.

2024-11-08 | PXD036778 | Pride

Nicotiana tabacum pollen tube lipid droplet proteome

Project description:The number of known proteins associated with plant lipid droplets (LDs) is small compared to other organelles. Many questions of LD biosynthesis and degradation remain open, also due to lack of candidate LD proteins whose characterization could help to elucidate their function in those processes. We performed a proteomic screen on LDs isolated from Nicotiana tabacum pollen tubes. Proteins that were highly enriched in the LD fraction compared to the total or cytosolic fraction where verified for LD localization via transient expression in tobacco pollen tubes.

2018-08-13 | PXD009184 | Pride

Nicotiana tabacum seed lipid droplet proteome

2018-08-13 | PXD009186 | Pride

Lipid droplet proteomics of THP1 macrophages infected with Mycobacterium tuberculosis

Project description:Growing evidence suggests the importance of lipid metabolism in pathogenesis of tuberculosis. Neutral lipids form the majority of lipids in caseous granulomas characteristic of tuberculosis. Macrophage lipid droplets form the store house of these lipids, yet infection induced changes in the proteome of these dynamic organelles remains elusive. Here we employed quantitative proteomics to identify alterations induced upon infection with live Mycobacterium tuberculosis in comparison with heat killed bacilli and uninfected macrophages. Association of specific proteins coupled with lysosomal function was found to be increased upon infection with live M. tuberculosis. Biochemical and microscopy based evidence validated the enrichment of the small GTPase Arl8b, the guanine nucleotide effector LAMTOR1, and the scavenger receptor SCARB2 on lipid droplets during live Mtb infection. We validated the localization of Arl8b on lipid droplets using super-resolution microscopy. Increased abundance of these lysosomal proteins on lipid droplets upon infection with live Mtb suggests active manipulation of the host lipid droplets by the pathogen. Furthermore, depletion of lipid droplets upon stable knockdown of diacylglycerol O-acyltransferase led to reduction in lysosomal acidification of infected cells, suggesting an active role of lipid droplets in lysosomal function during infection.

2019-11-14 | PXD008950 | Pride

Populus (P. tremula X tremuloides-'T89) Lipidbody proteome

Project description:Seed lipid bodies (LB), previously viewed as paradigmatic, possess a restricted proteome and serve carbon and energy storage. Albeit present in minute quantities, LBs are widespread in post-germinative tissues, where they display vigorous movement, mediate transient organellar interactions, and shuttle enzymes, and signaling molecules. Storage as well as motility and signaling are relevant in shoot meristems of woody perennials, which ahead of winter produce buds that like seeds establish dormancy, dehydrate, express OLEOSIN genes and accumulate LBs. Unlike seeds, buds do not completely desiccate and LBs retain potential signaling functions. Here, we mapped bud LB production under dormancy-inducing conditions. We found that over an 8-week period LBs enlarged significantly. Concomitantly, three major OLEOSIN family genes were transiently upregulated at the start of bud formation, while in their wake expression of lipid biosynthesis gene DGAT1a/b and lipase gene SDP1a/b increased. In parallel, LDAPa/b, LDAP2a, and LDAP3a/b were upregulated, especially LDAP1b. All LDAPs were localized to LBs. The conclusion that OLEOSINs were replaced by LDAPs was supported by the finding that PUX10a, PUX10b and CDC498A1, involved in OLESOSIN ubiquitination and degradation, were significantly upregulated. Our proteomic analysis identified 723 putative LB proteins. These included LB-anchored Caleosin and LDIP, peripherally associated LDAP1/3 and OBL1, and numerous proteins that reflect storage, transport, organellar interaction, opportunistic cargo and contaminants. There is a significant overlap with proteins identified earlier in plasmodesmal proteomes. Collectively, the data support a model in which LBs are part of a pre-installed mechanism that serves dormancy release, survival through winter and regrowth.

2021-06-29 | PXD020099 | Pride

Proteomic characterization of LDIP mutant phenotypes in Arabidopsis seedlings

Project description:Lipid droplets (LDs) are unique, protein-coated organelles found in all eukaryotic organisms that function primarily in the storage of energy-rich neutral lipids, such as triacylglycerols (TAGs). In plants, LDs are found in high abundance in oilseeds, and proteins involved in their formation and activity, such as oleosins, have been well-characterized. Our understanding of LD biogenesis and activity in other cell types, as well as the proteins that regulate these processes, is not as comprehensive. We recently identified and characterized a novel Arabidopsis LD coat protein termed LDIP (LDAP-interacting protein) that regulates LD size and neutral lipid homeostasis in leaf and seed embryonic cells. Here, we show that LDIP plays a distinct role in regulating LD size during biogenesis in leaf cells via interactions with key biogenetic proteins. Localization experiments performed in both plant and insect cells revealed LDIP is necessarily recruited to the LD surface by LDAP3 and binds nascent LDs during early-stage LD formation. Pull-down and Y2H assays indicate LDIP interacts with the biogenetic proteins SEIPINs, while combinatory expression levels of these proteins resulted in aberrant LD size and number in both plant cells and yeast. Evidence is also provided that LDIP plays a key role in modulating phospholipid levels in both leaves and seeds. Taken together, our data allow for the generation of model for LD biogenesis in non-seed cell types.

2022-02-15 | PXD012992 | Pride

Arabidopsis LDIP is an LDAP-interacting protein that influences lipid droplet biogenesis and neutral lipid homeostasis in both leaves and seeds

Project description:Cytoplasmic lipid droplets (LDs) are found in all types of plant cells where they are derived from the endoplasmic reticulum (ER) and function as a repository for neutral lipids, as well as serving in lipid remodelling and signalling. However, the mechanisms underlying the formation and functioning 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 LD biogenesis and neutral lipid homeostasis in vegetative tissues. Here, we screened a yeast two-hybrid library using Arabidopsis LDAP3 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 -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 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 seed oil amounts. Collectively, these data identify LDIP as a new player in LD biogenesis in plants that modulates both LD size and cellular neutral lipid homeostasis. Potential mechanisms of LDIP activity are discussed.

2017-11-06 | PXD007192 | Pride

A proteomics approach to study the role of lipid droplets in plant defense

Project description:Lipid Droplets (LDs), classically viewed as lipid storage particles, are recently emerging as dynamic organelles associated with stress responses and development; however, their involvement in plant immunity has been little investigated. Here we studied LDs in Arabidopsis thaliana leaves that respond to Pseudomonas syringae pv. tomato DC3000 avrRpm1 by inducing a hypersensitive defense reaction (HR), as well as during senescence. We established a protocol to reproducibly isolate LDs from a limited amount of tissue and performed a proteomic analysis of LDs from Pseudomonas-infected (for 24 h and 72 h) and senescent leaves. The proteomes defined shared ~50% similarity, with an enrichment of proteins associated with the Gene Ontology terms “transport” and “responses to stress”. As validation, we confirmed LD localization of glycerol-3-phosphate-acetyltransferase 8 (GPAT8) and GPAT4, enzymes required for e.g., cutin biosynthesis, by transient expression of GFP fusions in HR-induced leaves of Nicotiana benthamiana. Similarly, we proved the localization to LDs of aldehyde dehydrogenase 3F1 (ALDH3F1), α-dioxygenase1 (α-DOX1) and caleosin3 (CLO3), all involved in the synthesis of fatty acid derivatives. Moreover, we found that PAD3 (phytoalexin deficient 3) was distributed in patches along the ER and plasma membrane, and in LDs near dead cells. The nature of these proteins and of the additional components characterized in the LDs, together with the phenotypic examination of selected mutants, established a functional link between LDs and plant immunity. Our data suggest that these organelles participate in protein trafficking and in lipid changes that affect the interaction of plants with invading pathogens.

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A streamlined data analysis pipeline for the identification of sites of citrullination

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