Browse
Submit Data
Databases
API
Help

Dataset Information

399 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Nicotiana tabacum pollen tube lipid droplet proteome

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Nicotiana Tabacum (common Tobacco)

TISSUE(S): Plant Cell, Pollen Tube

SUBMITTER: Till Ischebeck

LAB HEAD: Dr. Till Ischebeck

PROVIDER: PXD009184 | Pride | 2018-08-13

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	170816uniproNtabacum.fasta	Fasta
	MaxQuant.exe	Other
	MaxQuant_Output.zip	Other
	TI16.raw	Raw
	TI17.raw	Raw

Items per page:

1 - 5 of 14

Publications

PUX10 Is a Lipid Droplet-Localized Scaffold Protein That Interacts with CELL DIVISION CYCLE48 and Is Involved in the Degradation of Lipid Droplet Proteins.

Kretzschmar Franziska K FK Mengel Laura A LA Müller Anna O AO Schmitt Kerstin K Blersch Katharina F KF Valerius Oliver O Braus Gerhard H GH Ischebeck Till T

The Plant cell 20180807 9

The number of known proteins associated with plant lipid droplets (LDs) is small compared with other organelles. Many aspects of LD biosynthesis and degradation are unknown, and identifying and characterizing candidate LD proteins could help elucidate these processes. Here, we analyzed the proteome of LD-enriched fractions isolated from tobacco (<i>Nicotiana tabacum</i>) pollen tubes. Proteins that were highly enriched in comparison with the total or cytosolic fraction were further tested for LD ...[more]

PMID: 30087207

Similar Datasets

Nicotiana tabacum seed 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. We also compared the isoforms of typical LD proteins found in the pollen tubes on a qualitative level to the isoforms found in tobacco seeds.

2018-08-13 | PXD009186 | Pride

Proteome of Arabidopsis thaliana pux10-1 mutant lipid droplets

Project description:The analysis of proteins isolated from whole seedling homogenate allowed insight into the abundance of lipid droplet proteins in different lines and time points. In order to gain more detailed insight into the protein composition of LDs of the different mutant lines and to increase the chances for the detection of post-translationally modified peptides, LD-enriched fractions were analyzed in a second proteomic approach. The LD fraction was isolated from homogenized seedlings of qrt PUX10, qrt pux10-1, C#1, and C#2 at 2 dai.

2018-08-13 | PXD009248 | 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

Proteome of Arabidopsis thaliana pux10-1 mutant lipid droplets at 1 and 2 days after imbibition

2018-08-13 | PXD009247 | 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

Seedling proteome of Arabidopsis thaliana pux10-1 mutants

Project description:Lipid droplets (LD) of seedlings lacking PUX10 stay significantly smaller during germination than the LDs of wild type seedlings. The observation that the removal of a LD-associated protein from a plant affects LD morphology has been observed previously {Siloto et al., 2006}{Gidda et al., 2016}. Especially the effect of the knock-out of the major structural LD protein Oleosin1 leading to a strongly increased size of LDs described by Siloto et al. might indicate that the abundance of structural LD proteins influences the LD size. Thus, the influence of the absence of PUX10 on the abundance of these proteins was investigated via a proteomic approach. Here, proteins isolated from homogenized seedlings of different lines (qrt PUX10, qrt pux10-1, complemented 1, and complemented 2) and different developmental stages (wet seeds, and 1 to 3 days after imbibition (dai)) were subjected to tryptic digest and LC-MS/MS analysis.

2018-08-13 | PXD009207 | Pride

Transcription profiling of Arabidopsis pollen and semi in vivo- and in vitro-grown pollen tubes.

Project description:Pollen tubes extend through pistil tissues and are guided to ovules where they release sperm for fertilization. Although pollen tubes can germinate and elongate in a synthetic medium, their trajectory is random and their growth rates are slower compared to growth in pistil tissues. Furthermore, interaction with the pistil renders pollen tubes competent to respond to guidance cues secreted by specialized cells within the ovule. The molecular basis for this potentiation of the pollen tube by the pistil remains uncharacterized. We used a surgical procedure to obtain large quantities of uncontaminated pollen tubes that grew through the pistil and defined their transcriptome by microarray analysis. We also characterized the transcriptome of in vitro-grown pollen tubes (for 0.5hours or 4hours) and dessicated mature pollen in Arabidopsis. Experiment Overall Design: Pollen and pollen tubes were collected as described in the protocols section for RNA extraction and hybridization on Affymetrix ATH1 Genechip microarrays.

2009-08-15 | E-GEOD-17343 | biostudies-arrayexpress

Proteomic analysis of secretions from pollen tubes and ovaries of Camellia oleifera cultured semi-in vivo

Project description:Self-inhibition of pollen tubes plays a key role in SI, but the underlying mechanism in Camellia oleifera is poorly understood. Collection of secreted proteins from Camellia oleifera pollen tubes and ovaries for high-throughput sequencing.

2023-03-11 | PXD035406 | Pride

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

Identification of a lipid droplet-plasma membrane tethering complex

Project description:Membrane contact sites (MCS) are interorganellar contacts that allow for the direct exchange of molecules such as lipids or Ca2+ between organelles, but can also be a mean for tethering of organelles. In mammals and yeast, LDs have been shown to engage in MCS with nearly all organelles in the cell, while in plants only LD-ER and LD-peroxisome contacts have been characterised. We here analyse three proteins, LD-localised SEED LIPID DROPLET PROTEIN (SLDP) 1 and 2 and PM-localised LIPID DROPLET PLASMA MEMBRANE ADAPTOR. Knockout of SLDP1 and 2, as well as knockout of LIPA lead to aberrant clustering of LDs in seedlings, while ectopic co-expression of SLDP and LIPA in Nicotiana tabacum pollen tubes is sufficient to reconstitute LD-PM tethering in this tissue, where LDs normally dynamically float in the cytosol stream. We propose a model, in which SLDP and LIPA interact and thereby form a tether to anchor a subset of LDs to the PM during post-germinative growth in Arabidopsis thaliana.

2022-06-09 | PXD022769 | Pride