C7orf43
- Known as:
- C7orf43
- Catalog number:
- 003263A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- C7orf43
Related genes to: C7orf43
- Gene:
- MAP11 NIH gene
- Name:
- microtubule associated protein 11
- Previous symbol:
- C7orf43
- Synonyms:
- FLJ10925
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-08-08
- Date modifiied:
- 2019-02-11
Related products to: C7orf43
Related articles to: C7orf43
- Thiazolopyridines are a highly relevant class of small molecules, which have previously shown a wide range of biological activities. Besides their anti-tubercular, anti-microbial and anti-viral activities, they also show anti-cancerogenic properties, and play a role as inhibitors of cancer-related proteins. Herein, the biological effects of the thiazolopyridine AV25R, a novel small molecule with unknown biological effects, were characterized. Screening of a set of lymphoma (SUP-T1, SU-DHL-4) and B- acute leukemia cell lines (RS4;11, SEM) revealed highly selective effects of AV25R. The selective anti-proliferative and metabolism-modulating effects were observed in vitro for the B-ALL cell line RS4;11. Further, we were able to detect severe morphological changes and the induction of apoptosis. Gene expression analysis identified a large number of differentially expressed genes after AV25R exposure and significant differentially regulated cancer-related signaling pathways, such as VEGFA-VEGFR2 signaling and the EGF/EGFR pathway. Structure-based pharmacophore screening approaches using in silico modeling identified potential biological AV25R targets. Our results indicate that AV25R binds with several proteins known to regulate cell proliferation and tumor progression, such as FECH, MAP11, EGFR, TGFBR1 and MDM2. The molecular docking analyses indicates that AV25R has a higher binding affinity compared to many of the experimentally validated small molecule inhibitors of these targets. Thus, here we present in vitro and in silico analyses which characterize, for the first time, the molecular acting mechanism of AV25R, including cellular and molecular biologic effects. Additionally, this predicted the target binding of the molecule, revealing a high affinity to cancer-related proteins and, thus, classified AVR25 for targeted intervention approaches. - Source: PubMed
Publication date: 2023/12/15
Ladwig AnnikaGupta ShailendraEhlers PeterSekora AnettAlammar MoosheerKoczan DirkWolkenhauer OlafJunghanss ChristianLanger PeterMurua Escobar Hugo - The primary cilium is a cellular sensor that detects light, chemicals, and movement and is important for morphogen and growth factor signaling. The small GTPase Rab11-Rab8 cascade is required for ciliogenesis. Rab11 traffics the guanine nucleotide exchange factor (GEF) Rabin8 to the centrosome to activate Rab8, needed for ciliary growth. Rabin8 also requires the transport particle protein complex (TRAPPC) proteins for centrosome recruitment during ciliogenesis. Here, using an MS-based approach for identifying Rabin8-interacting proteins, we identified C7orf43 (also known as microtubule-associated protein 11 (MAP11)) as being required for ciliation both in human cells and zebrafish embryos. We find that C7orf43 directly binds to Rabin8 and that C7orf43 knockdown diminishes Rabin8 preciliary centrosome accumulation. Interestingly, we found that C7orf43 co-sediments with TRAPPII complex subunits and directly interacts with TRAPPC proteins. Our findings establish that C7orf43 is a TRAPPII-specific complex component, referred to here as TRAPPC14. Additionally, we show that TRAPPC14 is dispensable for TRAPPII complex integrity but mediates Rabin8 association with the TRAPPII complex. Finally, we demonstrate that TRAPPC14 interacts with the distal appendage proteins Fas-binding factor 1 (FBF1) and centrosomal protein 83 (CEP83), which we show here are required for GFP-Rabin8 centrosomal accumulation, supporting a role for the TRAPPII complex in tethering preciliary vesicles to the mother centriole during ciliogenesis. In summary, our findings have revealed an uncharacterized TRAPPII-specific component, C7orf43/TRAPPC14, that regulates preciliary trafficking of Rabin8 and ciliogenesis and support previous findings that the TRAPPII complex functions as a membrane tether. - Source: PubMed
Publication date: 2019/08/29
Cuenca AdrianInsinna ChristineZhao HuijieJohn PeterWeiss Matthew ALu QuanlongWalia VijaySpecht SuzanneManivannan SelvambigaiStauffer JimmyPeden Andrew AWestlake Christopher J - Microtubule associated protein 11 (MAP11, previously termed C7orf43) encodes a highly conserved protein whose function is unknown. Through genome-wide linkage analysis combined with whole exome sequencing, we demonstrate that human autosomal recessive primary microcephaly is caused by a truncating mutation in MAP11. Moreover, homozygous MAP11-orthologue CRISPR/Cas9 knock-out zebrafish presented with microcephaly and decreased neuronal proliferation, recapitulating the human phenotype. We demonstrate that MAP11 is ubiquitously transcribed with high levels in brain and cerebellum. Immunofluorescence and co-immunoprecipitation studies in SH-SY5Y cells showed that MAP11 associates with mitotic spindles, co-localizing and physically associating with α-tubulin during mitosis. MAP11 expression precedes α-tubulin in gap formation of cell abscission at the midbody and is co-localized with PLK1, a key regulator of cytokinesis, at the edges of microtubule extensions of daughter cells post cytokinesis abscission, implicating a role in mitotic spindle dynamics and in regulation of cell abscission during cytokinesis. Finally, lentiviral-mediated silencing of MAP11 diminished SH-SY5Y cell viability, reducing proliferation rather than affecting apoptosis. Thus, MAP11 encodes a microtubule-associated protein that plays a role in spindle dynamics and cell division, in which mutations cause microcephaly in humans and zebrafish. - Source: PubMed
Perez YonatanBar-Yaacov ReutKadir RotemWormser OhadShelef IlanBirk Ohad SFlusser HagitBirnbaum Ramon Y - ABSTRACT Blacklegged ticks, Ixodes scapularis Say, were collected from 27 sites in eight New York State counties from 2003 to 2006 to determine the prevalence and distribution of tick-borne pathogens in public-use areas over a 4-yr period. In total, 11,204 I. scapularis (3,300 nymphs and 7,904 adults) were individually analyzed using polymerase chain reaction to detect the presence of Borrelia burgdorferi (causative agent of Lyme disease), Anaplasma phagocytophilum (formerly Ehrlichia phagocytophila, causative agent of human granulocytic anaplasmosis), and Babesia microti (causative agent of human babesiosis). Overall prevalence of B. burgdorferi, A. phagocytophilum, and B. microti was 14.4, 6.5, and 2.7% in nymphs and 45.7, 12.3, and 2.5% in adult ticks, respectively. Rates varied geographically and temporally during the time period examined, and were related to measurements of tick density. Average rate ofpolymicrobial infection for nymphs and adults, respectively, was 1.5 and 8.5% overall, with 0.5 and 6.3% coinfection of B. burgdorferi and A. phagocytophilum, 1.0 and 1.5% B. burgdorferi and B. microti, and 0.05 and 0.6% A. phagocytophilum and B. microti. Thirty-three individual adult ticks from seven study sites in Westchester, Putnam, Dutchess, and Rockland counties tested positive for simultaneous infection with all three agents by multiplex polymerase chain reaction assay. - Source: PubMed
Prusinski M AKokas J EHukey K TKogut S JLee JBackenson P B - Ehrlichia ruminantium, a tick-transmitted pathogen, is the causative agent of heartwater in ruminants. In this study, a proteomic approach was used to identify host cell-specific E. ruminantium proteins encoded by the map1 multigene family, expressed in vitro in bovine endothelial and tick cell cultures. Two-dimensional gel electrophoresis combined with mass spectrometry analysis was used to establish the identities of immunodominant proteins. Proteins extracted from E. ruminantium-infected endothelial cells were shown to be products of the map1 gene, whereas tick cell-derived E. ruminantium proteins were products of a different gene, map1-1. The expressed proteins were found to be glycosylated. Differential expression of MAP1 family proteins in vitro in mammalian and tick cell cultures indicates that the map1 multigene family might be involved in the adaptation of E. ruminantium to the mammalian host and vector tick. - Source: PubMed
Publication date: 2007/10/06
Postigo MTaoufik ABell-Sakyi LBekker C P Jde Vries EMorrison W IJongejan F