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APEX2 labeling of Sec bodies in S2 cells

ABSTRACT: APEX2 was tagged to Sec24AB protein in S2 cells. Biotinylation was triggeredin resting cells and amino acid starved cells for comparative analyses of Sec24AB interactome. Sec24AB is localised to Sec bodies during starvation, thereby allowing the identification of protein components in Sec bodies.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: wei wu

LAB HEAD: Wei Wu

PROVIDER: PXD031601 | Pride | 2023-05-10

REPOSITORIES: Pride

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			Action	DRS
	20201210_OR15_Ag5_wu000024_SA_CJ_APEX2_1_1.raw	Raw
	20201210_OR15_Ag5_wu000024_SA_CJ_APEX2_1_2.raw	Raw
	20201210_OR15_Ag5_wu000024_SA_CJ_APEX2_1_3.raw	Raw
	20201210_OR15_Ag5_wu000024_SA_CJ_APEX2_2_1.raw	Raw
	20201210_OR15_Ag5_wu000024_SA_CJ_APEX2_2_2.raw	Raw

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Publications

Novel Components of the Stress Assembly Sec Body Identified by Proximity Labeling.

Zhang Chujun C Kalaitsidou Elisavet E Damen J Mirjam A JMA Grond Rianne R Rabouille Catherine C Wu Wei W

Cells 20230330 7

Sec bodies are membraneless stress-induced assemblies that form by the coalescence of endoplasmic reticulum exit sites (ERES). Through APEX2 tagging of Sec24AB, we biotinylated and identified the full complement of Sec body proteins. In the presence of biotin-phenol and H2O2 (APEX on), APEX2 facilitates the transfer of a biotin moiety to nearby interactors of chimeric Sec24AB. Using this unbiased approach comparing APEX on and off (-H2O2) conditions, w ...[more]

PMID: 37048128

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Transcriptome of Drosophila S2 cells stressed upon amino-acid starvation in KRB (Krebs Ringer Bicarbonate)

Project description:The phase separation of the non-membrane bound Sec bodies occurs in Drosophila S2 cells by coalescence of components of the ER exit sites under the stress of amino-acid starvation. Here we provide the comparison of the gene expression profiles of S2 cells grown in full medium (Schneider's) and S2 cells upon of amino-acid starvation in KRB

2020-01-17 | GSE143810 | GEO

SEC

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Nano-structural analysis of engrafted human induced pluripotent stem cell-derived cardiomyocytes in mouse hearts using a genetic-probe APEX2.

Project description:Using APEX2, an engineered peroxidase, as an imaging tag, we successfully located iPSC-derived cardiomyocytes (iPSC-CMs) engrafted in post-myocardial infarction mouse hearts for more than 6 months. APEX2 caused clear contrast in X-ray microscopy and electron microscopy, and relatively well organized sarcomere structures were formed in iPSC-CMs. Electron microscopic tomography further found the development of T-tubules and dyads in APEX2-labelled cells, which are the signature characteristics of the maturation of cardiomyocytes.

2018-12-01 | GSE99470 | GEO

Gene target specificity of the Super Elongation Complex (SEC) family: How HIV-1 Tat employs selected SEC members to activate viral transcription

Project description:The AF4/FMR2 proteins AFF1 and AFF4 act as a scaffold to assemble the Super Elongation Complex (SEC) that strongly activates transcriptional elongation of HIV-1 and cellular genes. Although they can dimerize, it is unclear whether the dimers exist and function within a SEC in vivo. Furthermore, it is unknown whether AFF1 and AFF4 function similarly in mediating SEC-dependent activation of diverse genes. Providing answers to these questions, our current study shows that AFF1 and AFF4 reside in separate SECs that display largely distinct gene target specificities. While the AFF1-SEC is more potent in supporting HIV-1 transactivation by the viral Tat protein, the AFF4-SEC is more important for HSP70 induction upon heat shock. The functional difference between AFF1 and AFF4 in Tat-transactivation has been traced to a single amino acid variation between the two proteins, which causes them to enhance the affinity of Tat for P-TEFb, a key SEC component, with different efficiency. Finally, genome-wide analysis confirms that the genes regulated by AFF1- and AFF4-SEC are largely non-overlapping and perform distinct functions. Thus, the SEC represents a family of related complexes that exist to increase the regulatory diversity and gene control options during transactivation of diverse cellular and viral genes.

2015-05-20 | GSE69021 | GEO

Gene target specificity of the Super Elongation Complex (SEC) family: How HIV-1 Tat employs selected SEC members to activate viral transcription

2015-05-20 | E-GEOD-69021 | biostudies-arrayexpress

SEC-seq human plasma cells in nanovials

Project description:SEC-seq human plasma cells in nanovials

2023-05-23 | GSE229042 | GEO

The SEC family of RNA Polymerase II elongation factors: gene target specificity and transcriptional output

Project description:The elongation stage of transcription is a highly regulated in metazoan. We previously purified the AFF1/AFF4-containing Super Elongation Complex (SEC) as a major regulator of development and cancer pathogenesis. Here, we report the biochemical isolation of SEC-like 2 (SEC-L2) and SEC-like 3 (SEC-L3) containing AFF2 and AFF3 in association with P-TEFb, ENL, and AF9. The SEC family members demonstrate high levels of Pol II CTD kinase activity, however, only SEC is required for the proper induction of the HSP70 gene upon stress. Genome-wide mRNA-seq analyses demonstrate that SEC-L2-3 control the expression of different subsets of genes, while AFF4/SEC plays a more dominant role in rapid gene expression in cells. MYC is one of the direct targets of AFF4/SEC, and the SEC requirement to the MYC gene regulates its expression in different cancer cells bearing either acute myeloid or lymphoid leukemia. These findings suggest that AFF4/SEC could be a potential therapeutic target for the treatment of leukemia or other cancers associated with MYC overexpression.

2012-05-02 | GSE34097 | GEO

Project description:S2 Metagenome data

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Bacillus velezensis strain:SEC-024A

Project description:Bacillus velezensis strain:SEC-024A Genome sequencing

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Targeting Processive Transcription Elongation via SEC Disruption for MYC-Induced Cancer Therapy

Project description:The super elongation complex (SEC) is required for robust and productive transcription through release of RNA polymerase II (Pol II) with its P-TEFb module and promoting transcriptional processivity with its ELL2 subunit. Malfunction of SEC contributes to multiple human diseases including cancer. Here, we identify peptidomimetic lead compounds, KL-1 and its structural homolog KL-2, which disrupt the interaction between the SEC scaffolding protein AFF4 and P-TEFb, resulting in impaired release of Pol II from promoter-proximal pause sites and a reduced average rate of processive transcription elongation. SEC is required for induction of heat-shock genes and treating cells with KL-1 and KL-2 attenuates the heat-shock response from Drosophila to human. SEC inhibition downregulates MYC and MYC-dependent transcriptional programs in mammalian cells and delays tumor progression in a mouse xenograft model of MYC-driven cancer, indicating that small-molecule disruptors of SEC could be used for targeted therapy of MYC-induced cancer.

2018-10-26 | GSE112608 | GEO

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