c_Jun (Phospho_Tyr170) Antibody
- Known as:
- c_Jun (Phospho_Tyr170) Antibody
- Catalog number:
- E011023-2
- Product Quantity:
- 100ug
- Category:
- Antibodies
- Supplier:
- EnoGene
- Gene target:
- c_Jun (Phospho_Tyr170) Antibody
Ask about this productRelated products to: c_Jun (Phospho_Tyr170) Antibody
Related articles to: c_Jun (Phospho_Tyr170) Antibody
- Chemotropism, the ability to orient growth toward external chemical cues, is a fundamental process in diverse eukaryotic systems. During mating, budding yeast cells detect pheromone gradients from potential partners, locating them by assembling a gradient-tracking machine (GTM) at the plasma membrane that redistributes upgradient prior to polarized growth. Although membrane lipids are known to influence pheromone signaling and morphogenesis, their roles in pre-morphogenic gradient tracking have remained unclear. Here, we show that phosphatidylserine (PS), phosphatidylinositol-4,5-bisphosphate, and ergosterol exhibit GTM-like dynamics, polarizing to the default polarity site, redistributing upgradient, and stabilizing at the chemotropic site. Blocking PS synthesis causes a severe and specific gradient-tracking defect, whereas disruption of Bem1 binding to anionic lipids slows but does not abolish tracking. Analysis of polarity, Cdc42 activity, and exocyst dynamics indicates that Bem1 membrane binding contributes to spatial focusing of Cdc42 activation during tracking but cannot account for the pronounced defects caused by PS loss, indicating that PS influences gradient tracking through multiple GTM components. In contrast, ergosterol is dispensable for tracking but required for proper receptor organization and partner alignment after GTM stabilization. Together, these findings establish membrane lipids as integral GTM components and highlight PS as a key regulator of chemotropic gradient sensing through multivalent protein-lipid interactions. - Source: PubMed
Publication date: 2026/05/05
Pai Chih-YuWang XinMahmood HamidaStone David E - Apical-basal polarity is essential for epithelial organization and function and is established by conserved cortical polarity proteins. However, the requirements for canonical polarity factors vary between tissues and organisms. For example, the basolateral protein lethal giant larvae is essential for epithelial polarity in Drosophila but dispensable in Caenorhabditis elegans. To better define the epithelial polarity program in C. elegans, we performed a genome-wide RNAi screen for synthetic lethality with lgl-1. Combined loss of LGL-1 and the RhoGAP PAC-1 caused embryonic lethality due to elongation defects and epidermal rupture. Epidermal cells showed expansion of the apical domain and aPKC, accompanied by mislocalization of junctional proteins and LET-413Scribble. These defects indicate overactivity of apical polarity determinants. Consistently, partial inactivation of aPKC or CDC-42 suppressed lethality in pac-1; lgl-1 animals. Together, our results identify PAC-1 and LGL-1 as redundant inhibitors of apical polarity in the C. elegans embryonic epidermis and provide new insights into how conserved mechanisms are adapted across species. - Source: PubMed
Publication date: 2026/05/05
JarosiĆska Olga DRiga AmaliaFahs Hala ZahreddineWoeltjes Joren MSchmidt RubenRefai Fathima SGopinadhan SumaGunsalus Kristin CBoxem Mike - Control of the local reaction environment at electrocatalytic interfaces is crucial for determining the activity and selectivity of many electrochemical reactions. Here, we demonstrate that single-stranded DNA (ssDNA) layers with anionic phosphate backbones can serve as ionomer-like coatings that modulate local pH. On gold nanoparticle (AuNP) electrocatalysts, ssDNA layers enable nanoscale control of the interfacial environment by independently controlling coating thickness through strand-length variation and internal phosphate backbone networking through sequence-encoded base-pairing interactions. We find that ssDNA layers modulate the activity and selectivity of hydroxide ion (OH)-involving reactions in a sequence-dependent manner on AuNPs, as exemplified by the hydrogen evolution and glycerol oxidation reactions. Through structure-activity analysis, temperature-dependent experiments, and ssDNA constructs with systematically varied base-pairing, we identify base-pairing interactions within ssDNA layers as the key determinant governing the catalytic behavior. Operando surface-enhanced Raman spectroscopy reveals an ssDNA-mediated regulation mechanism in which the anionic phosphate backbones induce Donnan exclusion of OH at the nanoscale interface, with the extent of OH buildup or replenishment strongly dependent on base-pairing interactions. Our results suggest ssDNA as a programmable platform for engineering nanoscale reaction environments and propose design principles for ionomer-like architectures in electrocatalysis. - Source: PubMed
Publication date: 2026/05/05
Oh Sang YeonLee Tae KyoungJun JaeyeonWoo JinseLee ChanghoKim YonghaPark Jimin - Proteins operate in crowded physiological environments, yet their conformational and oligomeric states are largely inferred from experiments performed under dilute buffer conditions. Here, we show that for lysozyme (LYS) and bovine serum albumin (BSA), self-crowding at physiologically relevant concentrations alters protein structure and assembly, leading to well-defined dense protein states. Circular dichroism reveals a pronounced yet reversible shift from -helices to -sheets and turns in both proteins, indicating structural changes that are stable but distinct from amyloid aggregation. Small-angle X-ray scattering shows that LYS exhibits net attractive interprotein interactions, whereas BSA displays dominant repulsions that destabilize its dimeric state. At low concentrations, BSA acts as a self-hydrotrope, stabilizing monomers through weak attractions, while at higher concentrations self-crowding promotes dimer dissociation through protein interface destabilization and solution reorganization. Together, these findings demonstrate that protein self-crowding drives reversible restructuring of protein conformation and interactions, challenging classical volume-exclusion models of macromolecular crowding. - Source: PubMed
Olgenblum Gil ILevy Yehonatan NHarries Daniel - Homelessness is a pressing worldwide social and health concern. People who are housed may not necessarily adapt to being at 'home' and return to homelessness. To learn more, this study explored and synthesised how people with lived experiences of homelessness described the concept of 'home'. A meta-ethnographic qualitative systematic review was conducted to provide insights for improving housing outcomes and person-centred policies and programmes. - Source: PubMed
Thornhill LeilaSellar BenHernandez Gabrielle RosaMurray Carolyn M