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Rab18 BioID Nov 24 2015 McGill University

ABSTRACT: BioID datasets of wt, Q and S in the absence and presence of oleate. Tetracyclin-induced Rab18-BirA* hybrid proteins stably expressed in HEK293 cells. Included also, NBirA* plus minus oleate induced and expressed as controls.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Tommy Nilsson

LAB HEAD: Tommy Nilsson

PROVIDER: PXD016631 | Pride | 2024-01-26

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	NBirACntrlOleic_4Tommy.sf3	Other
	NBirACntrlOleic_Band1.raw	Raw
	NBirACntrlOleic_Band1.raw.mgf	Mgf
	NBirACntrlOleic_Band1.raw.mgf.dat	Mgf
	NBirACntrlOleic_Band2.raw	Raw

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1 - 5 of 56

Publications

Comparative proximity biotinylation implicates the small GTPase RAB18 in sterol mobilization and biosynthesis.

Kiss Robert S RS Chicoine Jarred J Khalil Youssef Y Sladek Robert R Chen He H Pisaturo Alessandro A Martin Cyril C Dale Jessica D JD Brudenell Tegan A TA Kamath Archith A Kyei-Boahen Jeffrey J Hafiane Anouar A Daliah Girija G Alecki Célia C Hopes Tayah S TS Heier Martin M Aligianis Irene A IA Lebrun Jean-Jacques JJ Aspden Julie J Paci Emanuele E Kerksiek Anja A Lütjohann Dieter D Clayton Peter P Wills Jimi C JC von Kriegsheim Alex A Nilsson Tommy T Sheridan Eamonn E Handley Mark T MT

The Journal of biological chemistry 20230928 11

Loss of functional RAB18 causes the autosomal recessive condition Warburg Micro syndrome. To better understand this disease, we used proximity biotinylation to generate an inventory of potential RAB18 effectors. A restricted set of 28 RAB18 interactions were dependent on the binary RAB3GAP1-RAB3GAP2 RAB18-guanine nucleotide exchange factor complex. Twelve of these 28 interactions are supported by prior reports, and we have directly validated novel interactions with SEC22A, TMCO4, and INPP5B. Con ...[more]

PMID: 37774976

Similar Datasets

BirA*-RAB18 proximity biotinylation in HeLa cells

Project description:Proximity labelling using transient expression of the same exogenous BirA*-RAB18 construct in wild-type HeLa cells and in otherwise isogenic RAB3GAP1-, RAB3GAP2- and TRAPPC9-null HeLa cell lines.

2024-01-26 | PXD016336 | Pride

2’3’-cGAMP binds and activates Rab18 to promote cell migration

Project description:Cyclic dinucleotides serve as bacterial secondary messengers regulating sporulation, motility, biofilm formation and virulence. A nonsymmetric c-di-GAMP is firstly identified in bacteria to promote colonization, while mammalian 2’3’-cGAMP is synthesized by cGAS through binding and activating STING to trigger innate immune activation. However, pathophysiological function of 2’3’-cGAMP beyond innate immunity remains elusive. Here, we report 2’3’-cGAMP facilitates cell migration independent of STING and its innate immune function. 2’3’-cGAMP interactome analysis with a targeted shRNA-screen identifies the GTPase Rab18 as a direct 2’3’-cGAMP binding partner and effector in cell migration control. Mechanistically, 2’3’-cGAMP binds Rab18-S17, E36 and R92 residues to facilitate Rab18 activation and subsequently promotes FosB transcription in promoting cell migration. Low-dose doxorubicin induces 2’3’-cGAMP synthesis and facilitates cell migration in vitro and in vivo. Interestingly, lovastatin induces Rab18 phosphorylation abolishes 2’3’-cGAMP recognition to antagonize 2’3’-cGAMP induced cell migration. Together, our study reveals a novel 2’3’-cGAMP function in cell migration control beyond innate immunity via binding Rab18 that provides new insights into clinical applications of 2’3’-cGAMP.

2024-09-11 | GSE210490 | GEO

Rab18 is not necessary for lipid droplet biogenesis or turnover in human mammary carcinoma cells

Project description:Rab GTPases recruit peripheral membrane proteins and can define organelle identity. Rab18 localizes to the ER but also to the surfaces of lipid droplets (LDs), where it has been implicated in effector protein recruitment and in defining LD identity. Here, we studied Rab18 localization and function in SUM159 cells. Rab18 localized to the ER and to LD membranes upon LD induction, with the latter depending on the Rab18 activation state. In cells lacking Rab18, LDs were modestly reduced in size and numbers, but we found little evidence for Rab18 function in LD formation, LD turnover upon cell starvation, or the targeting of several proteins to LDs. We conclude that Rab18 is not a general, necessary component of the protein machinery involved in LD biogenesis or turnover, but instead likely plays a specialized role in specific cell types

2018-06-06 | PXD009683 | Pride

2’3’-cGAMP binds and activates Rab18 to promote cell migration

Project description:2’3’-cGAMP binds and activates Rab18 to promote cell migration

| PRJNA865774 | ENA

IFITM3 BioID Interactomes in B-ALL and MCL

Project description:To determine the roles of membrane associated IFITM3 in BCR-signalling in B-cell malignancies we expressed N-terminal BirA-IFITM3-Y20E fusion or BirA-EV control in patient derived B-ALL cells (PDX2) and Jeko1 Mantle cell lymphoma (MCL) cells. Additionally to examine the role of PIP3 binding residues in the conserved intracellular loop region a K83A/K104A mutated form of IFITM3-Y20E-BirA fusion and compared with basic patch unmutated.

2020-12-18 | PXD020697 | Pride

RAB18 impacts autophagy via lipid droplet-derived lipid transfer and is rescued by ATG9A

Project description:Autophagy is a lysosomal degradation pathway that mediates protein and organelle turnover and maintains cellular homeostasis. Autophagosomes transport cargo to lysosomes and their formation is dependent on an appropriate lipid supply. Here, we show that the knockout of the RAB GTPase RAB18 interferes with lipid droplet (LD) metabolism, resulting in an impaired fatty acid mobilization. The reduced LD-derived lipid availability influences autophagy and provokes adaptive modifications of the autophagy network, which include increased ATG2B expression and ATG12-ATG5 conjugate formation as well as enhanced ATG2B and ATG9A phosphorylation. Phosphorylation of ATG9A directs this transmembrane protein to the site of autophagosome formation and this particular modification is sufficient to rescue autophagic activity under basal conditions in the absence of RAB18. However, it is incapable of enabling an increased autophagy under inductive conditions. Thus, we illustrate the role of RAB18 in connecting LDs and autophagy, further emphasize the importance of LD-derived lipids for the degradative pathway, and characterize an ATG9A phosphorylation-dependent autophagy rescue mechanism as an adaptive response that maintains autophagy under conditions of reduced LD-derived lipid availability.

2020-01-29 | PXD013719 | Pride

LFQP of lysates from wild-type, RAB18-, TBC1D20-, RAB3GAP1- and RAB3GAP2-null RPE1 cells

Project description:These data are from two wild-type RPE1 clones (WT11, WT20), a RAB18-null clone, a TBC1D20-null clone, a RAB3GAP1-null clone and a RAB3GAP2-null clone, each analysed in triplicate.

2024-01-26 | PXD016326 | Pride

Comprehensive temporal protein dynamics during the diauxic shift in Saccharomyces cerevisiae, part 5

Project description:Yeast (Saccharomyces cerevisea) has served as a key model system in biology and as a benchmark for “omics” technology. Although near-complete proteomes of log phase yeast have been measured, protein abundance in yeast is dynamic, particularly during the transition from log to stationary phase. Defining the dynamics of proteomic changes during this transition, termed the diauxic shift, is important to understand the basic biology of proliferative versus quiescent cells. Here, we perform temporal quantitative proteomics to fully capture protein induction and repression during the diauxic shift. Accurate and sensitive quantitation at a high temporal resolution and depth of proteome coverage was achieved using TMT10 reagents and LC-MS3 analysis on an Orbitrap Fusion tribrid mass spectrometer deploying synchronous precursor selection (SPS). We devised a simple template matching strategy to reveal temporal patterns of protein induction and repression. Within these groups are functionally distinct groups of proteins such as those of glyoxylate metabolism, as well as many proteins of unknown function not previously associated with the diauxic shift (e.g. YNR034W-A and FMP16). We also perform a dual time-course to determine Hap2-dependent proteins during the diauxic shift. These data serve as an important basic model for fermentative versus respiratory growth of yeast and other eukaryotes and are a benchmark for temporal quantitative proteomics

2015-06-22 | PXD001338 | Pride

Comprehensive temporal protein dynamics during the diauxic shift in Saccharomyces cerevisiae, part 4

2015-06-20 | PXD001335 | Pride

BioID-proximity labeling of GATAD1 variants

Project description:To gain insights into the interactome of wild-type (WT) and S102P mutant GATAD1, we utilized the BioID method, which enables the study of protein-protein interactions. Specifically, we performed BioID proximity labeling experiments in stable Flp-In cells expressing different GATAD1 variants fused to BirA*_FLAG. These variants included BirA*_FLAG_GATAD1-WT, BirA*_FLAG_GATAD1-S102P, BirA*_FLAG_GATAD1-S102D, and BirA*_FLAG_GATAD1-S102A. By employing this approach, we aimed to characterize the protein interactors associated with these GATAD1 variants and gain insights into the functional consequences of the S102P mutation.

2024-02-15 | PXD043789 | Pride

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