Fli1 polyclonal antibody
- Known as:
- Fli1 pab (anti-)
- Catalog number:
- PAB9876
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- Fli1 polyclonal antibody
Related genes to: Fli1 polyclonal antibody
- Gene:
- FLI1 NIH gene
- Name:
- Fli-1 proto-oncogene, ETS transcription factor
- Previous symbol:
- -
- Synonyms:
- SIC-1, EWSR2
- Chromosome:
- 11q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-06-05
- Date modifiied:
- 2019-04-23
- Gene:
- FLII NIH gene
- Name:
- FLII actin remodeling protein
- Previous symbol:
- -
- Synonyms:
- FLI, FLIL, Fli1, MGC39265
- Chromosome:
- 17p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-11
- Date modifiied:
- 2019-01-21
Related products to: Fli1 polyclonal antibody
Related articles to: Fli1 polyclonal antibody
- The obligate intracellular pathogen, , establishes an intracellular niche within a host membrane-derived vacuole called the chlamydial inclusion. From within this inclusion, orchestrates numerous host-pathogen interactions, in part, by utilizing a family of type III secreted effectors, termed inclusion membrane proteins (Incs). Incs are embedded within the inclusion membrane, and some function to recruit host proteins to the inclusion. Two such recruited host proteins are eucine ich epeat lightless-1 nteracting rotein 1 (LRRF1/LRRFIP1) and its binding partner Flightless 1 (FLI1/FLII). Previously, LRRF1 has been shown to interact with Inc protein Ct226/CTL0478. This is the first study to examine interactions of FLI1 with candidate Incs or with LRRF1 during infection. We hypothesized that FLI1 recruitment to the inclusion would be dependent on LRRF1 localization. We demonstrated that FLI1 co-immunoprecipitated with Ct226 but only in the presence of LRRF1. Furthermore, FLI1 localized to the inclusion when LRRF1 was depleted via small interfering RNA, suggesting that FLI1 may have an alternative recruitment mechanism. We further developed a series of CRISPRi knockdown and complementation strains in serovar L2 targeting ct226 and co-transcribed candidate Incs, ct225 and ct224. Simultaneous knockdown of ct226, ct225, and ct224 prevented localization of both FLI1 and LRRF1 to the inclusion, and only complementation of ct226 restored their localization. Thus, we demonstrated Ct226 is critical for FLI1 and LRRF1 localization to the inclusion. Our results also indicate an LRRF1-independent localization mechanism for FLI1, which likely influence their mechanism(s) of action during chlamydial infection.IMPORTANCE is a leading cause of both bacterial sexually transmitted infections and preventable infectious blindness worldwide. As an obligate intracellular pathogen, has evolved multiple ways of manipulating the host to establish a successful infection. As such, it is important to understand host-chlamydial protein-protein interactions as these reveal strategies that uses to shape its intracellular environment. This study looks in detail at interactions of two host proteins, FLI1 and LRRF1, during chlamydial infection. Importantly, the series of CRISPR inference knockdown and complement strains developed in this study suggest these proteins have both independent and overlapping mechanisms for localization, which ultimately will dictate how these proteins function during chlamydial infection. - Source: PubMed
Publication date: 2024/10/15
Sturd Natalie AKnight Lindsey AWood Macy GDurham LegacyOuellette Scot PRucks Elizabeth A - Immunotherapy is a practical therapeutic approach in breast cancer (BRCA), and the role of FLI1 in immune regulation has gradually been unveiled. However, the specific role of FLI1 in BRCA was conflicted; thus, additional convincing evidence is needed. - Source: PubMed
Publication date: 2024/03/06
Pei JianyingPeng YingMa KexinLan ChunyanZhang TingtingLi YanChen XiaofangGao Huafang - Interleukin-1β is one of the most potent inducers of beta cell inflammation in the lead-up to type 1 diabetes. We have previously reported that IL1β-stimulated pancreatic islets from mice with genetic ablation of stress-induced pseudokinase TRB3(TRB3KO) show attenuated activation kinetics for the MAP3K MLK3 and JNK stress kinases. However, JNK signaling constitutes only a portion of the cytokine-induced inflammatory response. Here we report that TRB3KO islets also show a decrease in amplitude and duration of IL1β-induced phosphorylation of TAK1 and IKK, kinases that drive the potent NF-κB proinflammatory signaling pathway. We observed that TRB3KO islets display decreased cytokine-induced beta cell death, preceded by a decrease in select downstream NF-κB targets, including iNOS/NOS2 (inducible nitric oxide synthase), a mediator of beta cell dysfunction and death. Thus, loss of TRB3 attenuates both pathways required for a cytokine-inducible, proapoptotic response in beta cells. In order to better understand the molecular basis of TRB3-enhanced, post-receptor IL1β signaling, we interrogated the TRB3 interactome using coimmunoprecipitation followed by mass spectrometry to identify immunomodulatory protein Flightless homolog 1 (Fli1) as a novel, TRB3-interacting protein. We show that TRB3 binds and disrupts Fli1-dependent sequestration of MyD88, thereby increasing availability of this most proximal adaptor required for IL1β receptor-dependent signaling. Fli1 sequesters MyD88 in a multiprotein complex resulting in a brake on the assembly of downstream signaling complexes. By interacting with Fli1, we propose that TRB3 lifts the brake on IL1β signaling to augment the proinflammatory response in beta cells. - Source: PubMed
Publication date: 2023/05/11
Gonuguntla SumatiHumphrey Rohan KGorantla AkshitaHao ErgengJhala Ulupi S - miRNAs modulate gene expression and play critical functions as oncomiRs or tumor suppressors. The miR-182-3p is important in chemoresistance and cancer progression in breast, lung, osteosarcoma, and ovarian cancer. However, the role of miR-182-3p in cervical cancer (CC) has not been elucidated. - Source: PubMed
Publication date: 2023/03/23
Salmerón-Bárcenas Eric GenaroMendoza-Catalan Miguel AngelRamírez-Bautista Ángela UrayLozano-Santos Rafael AcxelTorres-Rojas Francisco IsraelÁvila-López Pedro AntonioZacapala-Gómez Ana Elvira - Fusion-transcription factors (fusion-TFs) represent a class of driver oncoproteins that are difficult to therapeutically target. Recently, protein degradation has emerged as a strategy to target these challenging oncoproteins. The mechanisms that regulate fusion-TF stability, however, are generally unknown. Using CRISPR-Cas9 screening, we discovered tripartite motif-containing 8 (TRIM8) as an E3 ubiquitin ligase that ubiquitinates and degrades EWS/FLI, a driver fusion-TF in Ewing sarcoma. Moreover, we identified TRIM8 as a selective dependency in Ewing sarcoma compared with >700 other cancer cell lines. Mechanistically, TRIM8 knockout led to an increase in EWS/FLI protein levels that was not tolerated. EWS/FLI acts as a neomorphic substrate for TRIM8, defining the selective nature of the dependency. Our results demonstrate that fusion-TF protein stability is tightly regulated and highlight fusion oncoprotein-specific regulators as selective therapeutic targets. This study provides a tractable strategy to therapeutically exploit oncogene overdose in Ewing sarcoma and potentially other fusion-TF-driven cancers. - Source: PubMed
Publication date: 2021/07/29
Seong Bo Kyung ADharia Neekesh VLin ShanDonovan Katherine AChong ShashaRobichaud AmandaConway AmyHamze AmandaRoss LindaAlexe GabrielaAdane BiniamNabet BehnamFerguson Fleur MStolte BjörnWang Emily JueSun JialinDarzacq XavierPiccioni FedericaGray Nathanael SFischer Eric SStegmaier Kimberly