MYO1E antibody - N - terminal region (OAAB12067)
- Known as:
- MYO1E (anti-) - N - terminal region (OAAB12067)
- Catalog number:
- oaab12067
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- MYO1E antibody - terminal region (OAAB12067)
Related genes to: MYO1E antibody - N - terminal region (OAAB12067)
- Gene:
- MYO1E NIH gene
- Name:
- myosin IE
- Previous symbol:
- -
- Synonyms:
- MYO1C, HuncM-IC, MGC104638
- Chromosome:
- 15q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-04-04
- Date modifiied:
- 2015-07-22
Related products to: MYO1E antibody - N - terminal region (OAAB12067)
Related articles to: MYO1E antibody - N - terminal region (OAAB12067)
- Phagocytosis requires coordinated remodeling of the actin cytoskeleton to generate protrusive and contractile forces that drive target engulfment. Class I myosins Myo1e and Myo1f (Myo1e/f) have been implicated in linking the plasma membrane to the actin network, but their specific roles during Fc-receptor-mediated phagocytosis remain unclear. Using CRISPR-edited RAW 264.7 macrophages lacking Myo1e and Myo1f, we show that double knockout (dKO) cells exhibit markedly reduced uptake of IgG-coated beads, a phenotype that is partially rescued by re-expression of either myosin. Lattice-light-sheet and confocal imaging revealed distinct F-actin architectures corresponding to the various stages of cup progression, including basal podosome-like adhesions, individual phagocytic podosomes (actin teeth) along the rim of the cup, and a contractile phagocytic ring formed by the reorganization of podosomes into a higher-order network. In Myo1e/f-deficient cells, podosome formation was diminished, actin teeth were largely absent, and the phagocytic ring formed prematurely, which was often accompanied by stalled cup progression and repeated engulfment attempts. Myo1e/f localized both to podosomes and to the inner surface of the phagocytic ring, non-muscle myosin II (NM2) localized to the outer surface, and the absence of Myo1e/f correlated with the diffuse distribution of NM2. In addition, Myo1e/f-deficient macrophages exhibited increased trogocytosis of antibody-opsonized HL-60 cells, indicating a shift from whole-target engulfment toward partial target ingestion. These results suggest that Myo1e/f coordinate spatial and temporal transitions between protrusive and contractile actin networks, thereby ensuring efficient phagocytic cup progression. Our findings highlight a dual role for Myo1e/f in adhesion regulation and force balance during macrophage phagocytosis. - Source: PubMed
Publication date: 2026/05/01
Paul T CLoyd Y MChase S EO'Connor T WHobson C MLee R MVorselen DKrendel M - - Source: PubMed
Publication date: 2026/04/13
Xu MengqiOstap E Michael - Cholesterol must be precisely partitioned within cells, with the plasma membrane (PM) holding the highest levels. In contrast, the endoplasmic reticulum (ER)-the site of cholesterol synthesis-contains very little cholesterol. How newly synthesized cholesterol moves from the ER to the PM remains poorly defined. Here, we identify a COPII-independent trafficking route in which nascent cholesterol is exported via specialized cholesterol transport vesicles (CTVs). A genome-wide screen reveals that DEGS1-derived ceramide is essential for CTV formation at the ER. Biochemical purification shows that caveolins serve as the vesicle coat, and loss of caveolins eliminates CTV production. Silencing PACSINs or dynamins leads to intracellular accumulation of CTVs, suggesting impaired vesicle scission. CTV delivery to the PM depends on actin filaments and the motors MYO1C and MYO1E. In vitro reconstitution with giant unilamellar vesicles demonstrates that ceramide promotes inward budding, whereas CAV1 drives outward budding. This work identifies a previously unrecognized class of ER-derived, caveolin-coated vesicles that transport cholesterol to the PM. - Source: PubMed
Publication date: 2026/04/13
Sun MingLiu Yuan-BinSun Pu-YuSheng Zhao-ChenLiu Jia-WenYuan Pei-XinZhu Wen-ZhuoDeng GangWen Xing-YanZhao XiaoluLuo JieSong Bao-Liang - Temporal lobe epilepsy (TLE) remains a major clinical challenge, with over one-third of patients resistant to existing medications. Microglia, the brain's resident immune cells, are highly plastic, yet their potential to adopt a protective state in epilepsy is unclear. Using time-resolved single-nucleus RNA sequencing (snRNA-seq) in a kainic acid (KA)-induced seizure model, we identified an early-emerging microglial subpopulation transcriptionally distinct from homeostatic microglia. This subpopulation was characterized by high expression of insulin-like growth factor 1 (Igf1), along with Myo1e and Apbb2. Through in vitro co-culture assays, we demonstrated that TGFB1 stimulation, but not LPS, drives the generation of this IGF1 phenotype. These induced IGF1 microglia significantly suppressed the secretion of pro-inflammatory cytokines under inflammatory conditions. Importantly, conditioned medium from IGF1 microglia enhanced the proliferation and survival of KA-exposed HT22 neuronal-like cells. Mechanistically, we found that TGFB1 activates the Wnt/β-catenin pathway, promoting the nuclear translocation of β-catenin, which in turn upregulates IGF1 expression. In vitro, we abolished the TGFB1-induced neuroprotective phenotype by knocking down β-catenin using siRNA; however, exogenous supplementation with IGF1 partially rescued this effect. Our findings define a TGFB1-β-catenin-IGF1 axis that drives microglia into a neuroprotective state, revealing a novel endogenous mechanism and therapeutic direction for epilepsy. - Source: PubMed
Publication date: 2026/03/29
Yuan ZiweiLiu YanDuan RanZhang XiaogangHu LiqinSong FeiLiu JingMeng YuanKe PingyangXiao Fei - Steroid-resistant nephrotic syndrome (SRNS) in childhood frequently reflects monogenic podocytopathies in which immunosuppression is ineffective. Biallelic variants in , encoding the class I myosin Myo1E, cause a distinctive form of focal segmental glomerulosclerosis (FSGS) often accompanied by "Alport-like" multilamination of the glomerular basement membrane (GBM). Early recognition has therapeutic and prognostic implications. A previously healthy 4-year-old boy presented with generalized edema and nephrotic-range proteinuria. Glucocorticoids induced no remission; sequential calcineurin inhibition (cyclosporine, then tacrolimus) and a single dose of ofatumumab yielded only transient, partial reductions in proteinuria. A first biopsy elsewhere showed FSGS with nonspecific IgM/C3 trapping; electron microscopy (EM) was not performed. At age 10, repeat biopsy with EM revealed ~30% segmental foot-process effacement, focal GBM thickening (to 1740 nm), irregular lamina densa multilamination, and lamellar duplications without immune-complex deposits-features highly suggestive of hereditary GBM disease. Targeted sequencing identified compound-heterozygous variants segregating in trans: a canonical splice-donor change (c.2785+1G>A) and a frameshift (c.3094_3097del; p.Thr1032Profs*73). Each parent was an unaffected heterozygous carrier; the sibling was negative. Supportive therapy with ramipril was continued. At last follow-up (January 2025), renal function was normal (serum creatinine 0.5 mg/dL; creatinine clearance 122 mL/min) with stable sub-nephrotic proteinuria (0.52 g/day; 16 mg/m per hour) and normotension. This case broadens clinicopathologic recognition of -associated nephropathy and highlights the teaching point that Alport-like GBM changes are not pathognomonic for type IV collagen disorders but may signal defects in podocyte cytoskeletal anchoring. - Source: PubMed
Publication date: 2026/03/20
Angioi AndreaPiras DolorettaLepori NicolaBianco PaolaFloris MatteoCabiddu GianfrancaBarreca AntonellaPani Antonello