Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

CROP: A Retromer- PROPPIN complex mediating membrane fission in the endo-lysosomal system

ABSTRACT: Endo-lysosomal compartments exchange proteins by fusing, fissioning, and through endosomal transport carriers. Thereby, they sort many plasma membrane receptors and transporters and control cellular signaling and metabolism. How the membrane fission events are catalyzed is poorly understood. Here, we identify the novel CROP complex as a factor acting at this step. CROP integrates PROPPIN Atg18 with a part of the endosome- and vacuole-associated retromer complex to generate a membrane fission device of much higher potency. We studied its activity in yeast, in human cells and on liposomes.

INSTRUMENT(S): LTQ Orbitrap Velos, Orbitrap Fusion, Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Patrice Waridel

LAB HEAD: Andreas Mayer

PROVIDER: PXD031244 | Pride | 2022-05-05

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	10548-49_QEx_Mascot_data.zip	Other
	180725_Courtellemont_10548.raw	Raw
	180725_Courtellemont_10549.raw	Raw
	20151106_7887A.raw	Raw
	20151106_7887B.raw	Raw

Items per page:

1 - 5 of 15

Publications

CROP: a retromer-PROPPIN complex mediating membrane fission in the endo-lysosomal system.

Courtellemont Thibault T De Leo Maria Giovanna MG Gopaldass Navin N Mayer Andreas A

The EMBO journal 20220425 10

Endo-lysosomal compartments exchange proteins by fusing, fissioning, and through endosomal transport carriers. Thereby, they sort many plasma membrane receptors and transporters and control cellular signaling and metabolism. How the membrane fission events are catalyzed is poorly understood. Here, we identify the novel CROP complex as a factor acting at this step. CROP joins members of two protein families: the peripheral subunits of retromer, a coat forming endosomal transport carriers, and mem ...[more]

PMID: 35466426

Similar Datasets

Cellular responses in yeast proteostasis mutants affected in diverse branches of the protein quality control system

Project description:Protein quality controls (PQC) systems rely on three main activities to prevent the accumulation of misfolded proteins upon stress conditions and aging: refolding, degradation and sequestration. In Saccharomyces cerevisiae the Hsp70 chaperone system plays a central role in protein refolding, while degradation is predominantly executed by the ubiquitin proteasome system (UPS). The sequestrases Hsp42 and Btn2 deposit misfolded proteins in cytosolic and nuclear inclusions. This activity prevents exhaustion of limited Hsp70 resources by restricting the accessibility of misfolded proteins upon sequestration. Sequestrase mutants therefore show negative genetic interactions with yeast Hsp70 co-chaperone mutants (fes1D hsp104D, DD) that suffer from low Hsp70 capacity. Growth of DDbtn2D mutants is highly temperature-sensitive and results in proteostasis breakdown at non-permissive temperatures. Here, we probed for the role of the UPS system in maintaining protein homeostasis in DDbtn2D cells, affected in two major PQC branches. We show that DDD cells induce expression of diverse stress-related pathways including the UPS to counteract the proteostasis defects. UPS dependent degradation of the stringent Hsp70 substrate Luciferase in the mutant cells mirrors such compensatory activities of the PQC system. However, the enhanced UPS activity does not improve but aggravates the phenotypes of DDbtn2D cells. Reducing UPS activity in the mutant by lowering the levels of functional 26S proteasomes improved growth, increased refolding yield of the Luciferase reporter and attenuated global stress responses. This indicates that an imbalance between Hsp70-dependent refolding and UPS-mediated degradation activities strongly affects protein homeostasis of yeast Hsp70 capacity mutants and contributes to their severe growth phenotypes.

2023-03-10 | PXD037835 | Pride

CSA-FLAG UV Treatment - TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A

Project description:SILAC comparison between CSA interactome before and after UV treatment.

2018-10-19 | PXD008863 | Pride

Cell type-specific transcriptional responses of Arabidopsis to salinity

Project description:Microarray data were generated to investigate the changes in gene expression for two cell types of the root: pericycle and cortical cells in response to salt treatment. The transcription profile of both cell types were also generated. Cell-types of interest expressing specifically Green Fluorescent Protein (GFP) were isolated from the rest of the root using fluorescence-activated cell sorting (FACS). 11 arrays were generated from plants grown in control and salt conditions. All seedlings grew in one tank were collected and correspond to one biological sample. Two control biological replicates were used for pericycle and 3 for cortical cells. By comparison from control microarray, 6 others arrays from salt treated plant (3 for each cell types) were used to identified salt responsive genes. The salt treatment was done on day 6 and 7 with increment of 25mM every 24h.

2014-04-10 | E-GEOD-44307 | biostudies-arrayexpress

Francisella tularensis DsbA mutant MS/SILAC analysis

Project description:Comparison of enriched membrane fractions of Francisella tularensis subsp. holarctica strain FSC200 and its DsbA mutant by SILAC analysis.

2018-01-15 | PXD007682 | Pride

TFG Cell-derived matrix proteome

Project description:Examining the effect of RNAi-mediated depletion of TFG on extracellular matrix secretion

2016-05-20 | PXD004175 | Pride

Abl subtrates using tyrosine phosphoproteomics

Project description:In this study, we have prepared a mouse embryonic fibrobalst (MEF) cell line stably expressing R367A mutant human Abl in which the native mouse Abl1 and Abl2 were genetically deleted. We have used these R367A mutant Abl cells in combination with mass spectrometry to identify phosphorylation targets of Abl. Below, we describe these findings and their potential biological significance.

2018-03-16 | PXD007118 | Pride

Depletion of Keratin8 affects tumorigenic potential of A431 cells via altering multiple signaling pathways

Project description:Keratins are the largest subgroup of intermediate filament proteins which are expressed in a tissue specific and differentiation state dependent manner. Apart from their mechanical functions, they have been shown to perform various regulatory roles. Most of these functions have been studied on keratin pair of 8/18 (K8/18) which is preferentially expressed in simple epithelia. The aberrant expression of this keratin pair has been correlated with increased invasiveness and poor prognosis of various squamous cell carcinomas (SCCs) including Skin SSCs. However the exact role it’s of aberrant expression in skin SCCs and associated mechanism remains elusive. To understand the role of K8/18 in skin SCC, ShRNA based stable K8 knockdown clones were generated in skin epidermoid carcinoma derived A431 cells which resulted in the decreased tumorigenic potential of these cells. Next, to decipher the molecular basis behind K8 mediated regulation of tumorigenic potential of A431 cells, TMT based total quantitative proteomics was performed for vector control and K8 knockdown clones (K8KD1/K8KD2). There were a total of 2952 proteins detected in the TMT based total quantitative proteomics, out of which, K8KD1 clone showed 140 proteins to be differentially expressed, whereas K8KD2 clone showed 119 proteins to be differentially expressed in comparison to vector control cells. Further, functional analysis of our data showed involvement of cell death and survival together with cellular movement pathway to be affected upon K8 knockdown. Altogether, the present data potentiates the role of K8 in neoplastic progression of skin SCC, together with the possible mechanism underlying the same.

2018-02-27 | PXD007206 | Pride

Arabidopsis AGO3 predominantly recruits 24-nucleotide small RNAs to regulate epigenetic silencing [miRNA-seq]

Project description:AGO3 predominantly bound 24-nt sRNAs with 5â?? terminal adenine. The spectrum of AGO3-associated sRNAs was different from those bound to AGO2. By contrast, approximately 30% of AGO3-bound 24-nt sRNAs overlapped with those bound to AGO4 and over 60% of AGO3-associated 24-nt sRNA enriched loci were identical to those of AGO4. In addition, expression of AGO3 driven by AGO4 native promoter partially complemented AGO4 function and rescued DNA methylation defect in ago4-1 background. Examination of AGO3 and AGO2 bound small RNAs with/without salt stress.

2016-05-31 | E-GEOD-78088 | biostudies-arrayexpress

Phosphoproteomic analysis of UBQLN2 mutant cells

Project description:In the project “Phosphoproteomic analysis of UBQLN2 mutant cells” by Laura Strohm, Zehan Hu, Jörn Dengjel, and Christian Behrends eight sets of SILAC experiments were performed, two times four biological replicates, comparing proteome and phosphoproteome of control and UBQLN2 mutant, patient-derived lymphoblasts (LCLs).

2022-06-28 | PXD029730 | Pride

Probing the ovarian cancer O-glycoproteome by the Macrophage Galactose like C-type Lectin (MGL): dissecting novel patterns of immune recognition

Project description:Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type O-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface which profoundly impacts anti-tumor immune recognition. The tumor associated glycan pattern may thus be regarded as a biomarker of immune modulation. In Epithelial Ovarian Cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnose and develop novel therapeutic interventions, respectively. The aim of this study was therefore to interrogate the ovarian cancer O-glycoproteome and identify tumor associated glycoproteins relevant in tumor-Dendritic Cell (DC) interactions, mediated by the MGL C-type lectin, recognizing the tumor associated Tn O-glycan. Here we present a strategy, employing a recombinant human MGL protein, to probe the ovarian cancer O-glycoproteome. This was achieved by a MGL Lectin Weak Affinity Chromatography (LWAC) approach using glycoengineered ovarian cancer cells and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis allowed us to identify the glycan structure/arrangement identified by MGL and furthermore to recognize potential MGL binders located at cell membrane, as expected, but also within the intracellular compartment and the matrisome, strongly suggesting that MGL in vivo could act as sensor of cellular distress/damage and modulator of DC motility. The tumor glycoproteins binders for MGL may become relevant as potential “onco-immune” biomarkers for EOC progression and prognosis. Furthermore, these results contribute to the design of glyco-immunogens for DC-based cancer immunotherapy.

2020-10-19 | PXD017510 | Pride