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Protein interactions with GFP-tagged cytoplasmic dynein-2 DATASET3

ABSTRACT: To identify those proteins interacting with the cytoplasmic dynein-2 using mammalian cell lines stably expressing GFP-tagged intermediate chain subunits, WDR34 (DYNC2I2) or WDR60 (DYNC2I1).

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: David Stephens

LAB HEAD: David Stephens

PROVIDER: PXD031156 | Pride | 2023-01-24

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	011215_Con_v_IC2_v_WDR34_v_WDR60.xlsx	Xlsx
	011215_Control_1-6.msf	Msf
	011215_IC2_1-6.msf	Msf
	011215_WDR34_1-6.msf	Msf
	011215_WDR60_1-6.msf	Msf

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1 - 5 of 29

Publications

Multiple interactions of the dynein-2 complex with the IFT-B complex are required for effective intraflagellar transport.

Hiyamizu Shunya S Qiu Hantian H Vuolo Laura L Stevenson Nicola L NL Shak Caroline C Heesom Kate J KJ Hamada Yuki Y Tsurumi Yuta Y Chiba Shuhei S Katoh Yohei Y Stephens David J DJ Nakayama Kazuhisa K

Journal of cell science 20230207 5

The dynein-2 complex must be transported anterogradely within cilia to then drive retrograde trafficking of the intraflagellar transport (IFT) machinery containing IFT-A and IFT-B complexes. Here, we screened for potential interactions between the dynein-2 and IFT-B complexes and found multiple interactions among the dynein-2 and IFT-B subunits. In particular, WDR60 (also known as DYNC2I1) and the DYNC2H1-DYNC2LI1 dimer from dynein-2, and IFT54 (also known as TRAF3IP1) and IFT57 from IFT-B contr ...[more]

PMID: 36632779

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Protein interactions with GFP-tagged cytoplasmic dynein-2 DATASET1

Project description:To identify those proteins interacting with the cytoplasmic dynein-2 using mammalian cell lines stably expressing GFP-tagged intermediate chain subunits, WDR34 (DYNC2I2) or WDR60 (DYNC2I1).

2023-01-24 | PXD031157 | Pride

Protein interactions with GFP-tagged cytoplasmic dynein-2 DATASET2

2023-01-24 | PXD031158 | Pride

Protein interactions with HA-tagged cytoplasmic dynein-2 DATASET1

Project description:To identify those proteins interacting with the cytoplasmic dynein-2 using mammalian cell lines stably expressing HA-tagged intermediate chain subunits, WDR34 (DYNC2I2) or WDR60 (DYNC2I1).

2023-01-24 | PXD031154 | Pride

Protein interactions with HA-tagged cytoplasmic dynein-2 DATASET2

2023-01-24 | PXD031153 | Pride

Protein interactions with HA-tagged cytoplasmic dynein-2 DATASET1

2023-01-24 | PXD031151 | Pride

Protein interactions with HA-tagged WDR60 in CEP170 knockout cells

Project description:To identify those proteins interacting with the WDR60 subunit of cytoplasmic dynein-2 using mammalian cell lines stably expressing HA-tagged intermediate chain subunit WDR60 (DYNC2I1).

2024-04-15 | PXD046844 | Pride

Chromatin immunoprecipitation of Drosophila Schneider 2 cells using NELF-E and NELF-B antibodies

Project description:ChIP-chip analysis of GAGA factor and NELF in Drosophila S2 cells

2008-04-04 | E-MEXP-1547 | biostudies-arrayexpress

Coupling p53 binding and nucleosome occupancy measurements at p53 binding sites

Project description:We were interested to explain why p53 binds some high affinity sites in contrast to other high affinity sites that are not bound by p53. p53 binding was measured using p53 ChIP-CHIP and in parallel nucleosome occupancy was measured on these same sites Comparison between p53 binding and nucleosome occupancy at p53 predicted binding sites ChIP-CHIP of p53 from MCF7EcoR under Basal conditions and MCF7EcoR treated with NCS (Activated) and Mononucleosomal extraction from MCF7sip53, MCF7EcoR under Basal conditions and MCF7EcoR treated with NCS (Activated) Expression analysis of MCF7sip53 and MCF7EcoR treated with NCS (Activated)

2010-08-09 | E-GEOD-22783 | biostudies-arrayexpress

Discovery of telomere repeat-binding factor in the malaria parasite Plasmodium falciparum

Project description:ChIP-seq experiments were performed for the putative telomere repeat-binding factor (PfTRF) in the malaria parasite Plasmodium falciparum strain 3D7. The gene encoding this factor (PF3D7_1209300) was endogenously tagged with either a GFP- or a 3xHA-tag and these transgenic parasite lines were used in ChIP-sequencing experiments. Sequencing of the ChIP and input libraries showed enrichment of PfTRF at all telomere-repeat containing chromosome ends (reference genome Plasmodium falciparum 3D7 from PlasmoDB version 6.1) as well as in all upsB var promoters.In addition,PfTRF was enriched at seven additional, intra-chromosomal sites and called in the PfTRF-HA ChIP-seq only. Plasmodium falciparum 3D7 parasites were generated with -GFP or -3xHA C-terminal tagged TRF (PF3D7_1209300). Nuclei were isolated from formaldehyde cross-linked schizont-stage transgenic parasites and used to prepare chromatin. Chromatin immunoprecipitations were performed using mouse anti-GFP (Roche Diagnostics, #11814460001) or rat anti-HA 3F10 (Roche Diagnostics, #12158167001). Sequencing libraries were prepared according to a Plasmodium-optimized library preparation procedure including KAPA polymerase-mediated PCR amplification.

2016-07-15 | E-GEOD-76537 | biostudies-arrayexpress

Translation profiling of Drosophila during early embryogenesis

Project description:Translational control is critical for early Drosophila embryogenesis and is exerted mainly at the gene-specific level. To understand the post-transcriptional regulation during Drosophila early embryonic development, we used the sucrose polysomal gradient analyses and GeneChip analysis to illustrate the translation profile of individual mRNAs. A paper was published in Genome Biology 2007 under the tile Global analyses of mRNA translational control during early Drosophila embryogenesis". Experiment Overall Design: In this study, we have fractionated embryo extracts from a series of early stages by sedimentation on sucrose density gradients and analyzed the RNA components of these fractions. Our analysis has focused on analyzing ribosomal density, generally and for individual transcripts, global translational activity during the first 10 hours after egg laying and coordination between transcription and translation regulation.

2008-03-14 | E-GEOD-5430 | biostudies-arrayexpress