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Immunoprecipitation of cellulose synthase complex

ABSTRACT: In order to deepen our understanding of cellulose biosynthesis, this study utilised immunoprecipitation techniques with CESA6 as the bait protein to explore the CSC and its interactors.

INSTRUMENT(S):

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

TISSUE(S): Plant Cell, Seedling

SUBMITTER: Ghazanfar Khan

LAB HEAD: Ghazanfar Khan

PROVIDER: PXD045340 | Pride | 2024-05-23

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	191114_LTI6b1.msf	Msf
	191114_LTI6b1.raw	Raw
	191114_LTi6b2.raw	Raw
	191114_LTi6b3.raw	Raw
	191114_YFP-CESA6-1.raw	Raw

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Publications

Tip Growth Defective1 interacts with the cellulose synthase complex to regulate cellulose synthesis in Arabidopsis thaliana.

Lampugnani Edwin R ER Persson Staffan S Khan Ghazanfar Abbas GA

PloS one 20240215 2

Plant cells possess robust and flexible cell walls composed primarily of cellulose, a polysaccharide that provides structural support and enables cell expansion. Cellulose is synthesised by the Cellulose Synthase A (CESA) catalytic subunits, which form cellulose synthase complexes (CSCs). While significant progress has been made in unravelling CSC function, the trafficking of CSCs and the involvement of post-translational modifications in cellulose synthesis remain poorly understood. In order to ...[more]

PMID: 38358988

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The protein interactomes of AtNHR2A and AtNHR2B unraveled common and specialized functions in plant immunity integrating distinct biological processes

Project description:AtNHR2A (Arabidopsis thaliana nonhost resistance 2A) and AtNHR2B (Arabidopsis thaliana nonhost resistance 2B) are two proteins required in nonhost resistance, a broad spectrum mechanism of plant immunity that protects plants against pathogens. AtNHR2A and AtNHR2B are localized to the cytoplasm, chloroplasts and other subcellular compartments of unknown identity. The multiple localizations of AtNHR2A and AtNHR2B, suggest that they are highly dynamic and versatile proteins likely participating in multiple biological processes. In spite of their importance, their specific functions have not been elucidated. Thus, to aid in the functional characterization of these proteins and identify the biological processes in which these proteins participate, we used immunoprecipitation coupled with mass spectrometry (IP-MS), to identify the proteins interacting with AtNHR2A and AtNHR2B and generate their interactome network. Further analysis of the AtNHR2A- and AtNHR2B-interacting proteins using published empirical information revealed that AtNHR2A and AtNHR2B function is not limited to plant immunity, highlighting that these proteins are hubs integrating defense outputs with other biological processes.

2020-03-10 | PXD015894 | Pride

Fungal COP9 signalosome assembly requires connection of two trimeric intermediates for integration of intrinsic deneddylase

Project description:The eight-subunit COP9 signalosome (CSN complex), controls the exchange of E3 ubiquitin cullin RING ligase receptors through its deneddylase activity, providing specificity to eukaryotic protein degradation. The conserved eight-subunit CSN complex is required for multicellular development of the filamentous fungus Aspergillus nidulans. The human, as well as the fungal CSN complex assembles through a heptameric subcomplex (pre-CSN complex) that is activated by the integration of the eighth subunit, the catalytic CsnE/5 deneddylase. The focus of this work was to unveil the assembly of the native fungal pre-CSN complex via combined genetic and biochemical approaches. Interactomes of various functional GFP-Csn subunit fusions, produced in pre-CSN deficient fungal double csn subunit gene deletion strains, were compared by affinity purifications coupled to mass spectrometry analyses. With this approach, two distinct heterotrimeric CSN subcomplexes were identified as pre-CSN assembly intermediates, namely CsnA/1-C/3-H/8 and CsnD/4-F/6-G/7 that form independently of CsnB/2 that connects the heterotrimers to a heptameric subcomplex and enables subsequent integration of CsnE/5, yielding in the enzymatically active CSN holocomplex. Surveillance mechanisms control accurate Csn subunit abundances and correct cellular localization for sequential assembly, since deprivation of Csn subunits change the abundance and location of the remaining Csn subunits.

2023-08-10 | PXD043205 | Pride

Nuclear mRNA quality control is bypassed for rapid export of stress responsive transcripts (Microarray)

Project description:Comparative analyses of Mex67 and Npl3 binding to mRNA at normal growth condition (25Â°C) and upon shift to heat stress (30 min, 42Â°C). Comparative analyses of mRNA binding of Mex67, Npl3 and no tag control at normal growth condition (25Â°C) and upon heat stress (30 min, 42Â°C) via RNA Co-IP experiments. Respective co-purified mRNAs were subjected to cDNA Microarray chips.

2016-06-14 | E-GEOD-83267 | biostudies-arrayexpress

Identification of potential interactors of COMPANION OF CELLULOSE SYNTHASE (CC) 1

Project description:Salt stress is one of the most detrimental abiotic stresses for plants. The plant cell wall, which encases plant cells and functions as a cellular exoskeleton, is an important structure to cope with such stresses. One of the main components of the cell wall is cellulose, which is synthesized by cellulose synthase (CESA) complexes (CSC) at the plasma membrane by moving along underlying cortical microtubules. COMPANION OF CELLULOSE SYNTHASE (CC) 1 and 2 have been identified to be components of the CSCs, and function in maintaining cellulose synthesis under salt stress by supporting microtubules and CESA behaviors. However, the exact regulatory mechanisms of the CC1 and CC2 proteins remain largely unknown. In this project, we did an immunoprecipitation-mass spectrometry (IP-MS) analysis to identify potential interactors of CC1 for further study.

2024-08-30 | PXD047667 | Pride

RNA-seq to investigate the phase separation-dependent FUS RNA interactome

Project description:The protein Fused in Sarcoma undergoes liquid-liquid phase separation. To investigate whether this phase transition alters the RNA interactome we purified phase-separated FUS droplets and soluble FUS from HEK 293T cells transfected with GFP-tagged WT FUS or P525L FUS. Phase separated FUS was purified by fluorescence-activated particle sorting (droplets) and soluble FUS by co-Immunoprecipitation (IP) respectively followed by isolation of co-purified RNA. Here we show that phase separation affects the RNA interactome of FUS.

2021-06-23 | E-MTAB-8456 | biostudies-arrayexpress

Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins

Project description:The aim of the MS analysis is to identify fatty acids modifying Cys3 of GNAI3 in cells exposed to high C16:0 or C18:0 concentrations. Detailed description in the manuscript Nuskova et al. submitted to NatComms.

2021-08-26 | PXD027064 | Pride

Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins

Project description:The aim of the MS analysis is to identify fatty acids modifying Cys3 of GNAI3. Detailed description in the manuscript Nuskova et al. submitted to NatComms.

2021-07-22 | PXD021517 | Pride

COLD6-OSM1 module senses chilling for the tolerance via 2',3'-cAMP signal in rice

Project description:To further elucidate how COLD6 regulates rice chilling tolerance, we investigated COLD6 interacting proteins using COLD6ind-GFP transgenic line by immunoprecipitation in combination with mass spectrometry (IP-MS). COLD6ind-GFP was applied to bind proteins in chilling-treated rice seedling samples, and the proteins bound at the plasma membrane were subsequently extracted for further analysis. We identified 44 potential interacted proteins with COLD6. Osmotin-like protein (OSM1, LOC_Os12g38170), known for its involvement in plant abiotic stress, was found in two independent experiments.

2024-11-02 | PXD049238 | Pride

COLD6-OSM1 module senses chilling for the tolerance via 2',3'-cAMP signal in rice

Project description:To further elucidate how COLD6 regulates rice chilling tolerance, we investigated COLD6 interacting proteins using COLD6ind-GFP transgenic line by immunoprecipitation in combination with mass spectrometry (IP-MS). COLD6ind-GFP was applied to bind proteins in chilling-treated rice seedling samples, and the proteins bound at the plasma membrane were subsequently extracted for further analysis. We identified 44 potential interacted proteins with COLD6.Osmotin-like protein (OSM1, LOC_Os12g38170), known for its involvement in plant abiotic stress, was found in two independent experiments.

2024-11-02 | PXD049115 | Pride

Usf1, a Suppressor of the Circadian Clock Mutant, Reveals the Nature of the DNA-binding of the CLOCK:BMAL1 complex in mice

Project description:Genetic and molecular approaches have been critical for elucidating the mechanism of the mammalian circadian clock. Here, we demonstrate that the ClockM-NM-^T19 mutant behavioral phenotype is significantly modified by mouse strain genetic background. We map a suppressor of the ClockM-NM-^T19 mutation to a M-bM-^HM-<900 kb interval on mouse chromosome 1 and identify the transcription factor, Usf1, as the responsible gene. A SNP in the promoter of Usf1 causes elevation of its transcript and protein in strains that suppress the Clock mutant phenotype. USF1 competes with the CLOCK:BMAL1 complex for binding to E-box sites in target genes. Saturation binding experiments demonstrate reduced affinity of the CLOCKM-NM-^T19:BMAL1 complex for E-box sites, thereby permitting increased USF1 occupancy on a genome-wide basis. We propose that USF1 is an important modulator of molecular and behavioral circadian rhythms in mammals. DOI:http://dx.doi.org/10.7554/eLife.00426.001. Examination of 3 transcriptional regulators in mouse liver at ZT8

2013-04-21 | E-GEOD-44609 | biostudies-arrayexpress

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