MYCBP Antibody
- Known as:
- MYCBP Antibody
- Catalog number:
- csb-ma8587101a0m
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- MYCBP Antibody
Related genes to: MYCBP Antibody
- Gene:
- MYCBP NIH gene
- Name:
- MYC binding protein
- Previous symbol:
- -
- Synonyms:
- AMY-1
- Chromosome:
- 1p34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-26
- Date modifiied:
- 2016-10-05
Related products to: MYCBP Antibody
Related articles to: MYCBP Antibody
- Chronic stress is increasingly recognized as a driver of cancer metabolism, highlighting the need to elucidate the mechanism linking chronic stress to metabolic reprogramming. Here, we performed untargeted metabolomics on serum samples from esophageal squamous cell carcinoma (ESCC) patients and integrated the results with clinical and stress-related assessments, revealing pentose phosphate pathway (PPP) enrichment accompanied by elevated epinephrine levels in patients with stress-associated features. β2-adrenergic receptor (ADRB2) activated by chronic stress stabilized MYCBP by competitively displacing VHL, thereby enhancing MYC transcriptional activity and upregulating key PPP enzymes, including G6PD and TKT. Unexpectedly, stress-associated stimulation not only activated ADRB2 signaling but also increased ADRB2 protein abundance. Mechanistically, stress exposure enhanced RNMT-dependent N7-methylguanosine (m7G) cap modification of ADRB2 mRNA, thereby increasing its translational efficiency. Together, these findings define an RNMT-ADRB2-MYCBP-PPP axis that integrates epitranscriptomic regulation with adrenergic signaling to promote metabolic reprogramming and malignant progression in ESCC. The stress-associated RNA modification-metabolism circuitry comprises potential therapeutic targets to overcome stress-associated ESCC progression. - Source: PubMed
Publication date: 2026/08/05
Zhang ZihanLiu FeifeiWang PengWang TingWang XiangyuWang RuiShi XiaodanZou RuixiaJia LudanWei XingLi ZhiboYu YankanSun HaiBoKim Dong JoonZhao SiminDong Zigang - miR-143-5p functions as a tumor-suppressive microRNA across various cancer types. The current study investigated the expression, prognostic value, and role of miR-143-5p in colorectal cancer (CRC). - Source: PubMed
Publication date: 2026/07/21
Mu ChenZhang Han - The central apparatus of motile cilia, consisting of central microtubules and various protein projections, is essential for dictating the ciliary movement. Although three proteins (FAP65, FAP147, and FAP70) have been localized to the C2a projection in , the full protein composition and functional roles of the vertebrate C2a remain inadequately defined. Here, we use three knockout mouse models corresponding to their respective homologs (, , and ) to systematically investigate their functions in vertebrates. Notably, all three knockout strains exhibit distinct phenotypes related to primary ciliary dyskinesia (PCD), including hydrocephalus and sinusitis. The ciliary incorporation of CCDC108, MYCBPAP, and CFAP70 is essential for one another's stability, with the loss of any single component triggering C2a collapse, which destabilizes the central pair microtubules, and ultimately alters the ciliary movement pattern. Furthermore, we significantly expand the vertebrate C2a proteome by identifying ARMC3 and MYCBP as additional C2a components. Collectively, our findings illuminate the proteomic composition and strict physiological requirements of the vertebrate C2a projection, providing new insights into the molecular pathogenesis of PCD. - Source: PubMed
Publication date: 2026/07/08
Lyu QianLi QingchaoLi JingruiLuo JiajunLiu ChunyuNai ShanshanLiu HongbinZhu XueliangSong TingLiu MinZhao Huijie - Papillary thyroid carcinoma (PTC) has shown a marked rise in incidence worldwide in recent decades, yet its molecular mechanisms remain largely unclear. Here, we reported that CBLB acts as a tumor suppressor in PTC. Analysis of public databases (GEPIA, UALCAN) and PTC cell lines confirmed reduced CBLB expression in tumor tissues compared to normal thyroid tissue. Functional experiments revealed that CBLB knockdown promoted malignant phenotypes, while its overexpression suppressed tumorigenic behaviors. Mechanistically, CBLB directly binds to MYCBP and promotes its poly-ubiquitination and proteasomal degradation via K48-linked ubiquitination at the K20 residue. MYCBP stabilization upon CBLB depletion activated the c-Myc pathway, upregulating oncogenic targets (CCND1, CDK4, ZEB1, E2F1, c-Jun) and downregulating E-cadherin. Collectively, our findings identify the CBLB/MYCBP/c-Myc axis as a critical regulatory pathway in PTC progression, highlighting CBLB's therapeutic potential as a targeted suppressor of MYCBP-driven oncogenesis. - Source: PubMed
Publication date: 2026/05/25
Yang YanliPei XiaoyanYang QingqingHu Xiaolei - The C2a projection of the central pair of flagella in Chlamydomonas reinhardtii harbours the A-kinase anchoring protein FAP65, FAP174, FAP147 and FAP70. FAP174, an RII-like protein with its N-terminal dimerization and docking domain, binds to the amphipathic helices of FAP65. Cryo-EM data do not reveal the entire sequences for FAP174 and FAP147. Hence, the interacting domains within this scaffold remain elusive. This study has identified the interacting domains of FAP174 with FAP147. The FAP147 protein and its MYCBPAP domain (129-639 a.a.) bind to the C-terminus of FAP174 (47-92 a.a.). In silico docking analyses using CABS-Dock to delineate the interaction identified several MYCBPAP-derived peptides, such as p3 (310-339), p4 (319-348), p9 (547-576), p13 (528-557) and p15 (350-379), to form stable interacting complexes with RMSD < 3 Å 2-3 times, and are potentially amphipathic. To gain atomistic details of the interaction, molecular dynamics (MD) simulations of the FAP147 MYCBPAP domain in complex with the FAP174 C-terminus were performed. It revealed stable interfacial contacts, a subset of which overlap with residues within the p15 peptide region of the MYCBPAP domain, while identifying G48, S49, P52, Y55, L79, Q80 and V83 as key interacting residues within the C-terminus of FAP174. Individual alanine substitution of the FAP174 residues, followed by overlay assay with FAP147, retained the interaction, indicating that the interaction does not depend solely on discrete amino acids but on broader interface interactions. - Source: PubMed
Publication date: 2026/02/22
Desai SnehaPal AbhayNair HridhyaDantu Sarath ChandraD'Souza Jacinta S