UNC84B Blocking Peptide
- Known as:
- UNC84B Blocking Peptide
- Catalog number:
- 33r-1831
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- UNC84B Blocking Peptide
Related genes to: UNC84B Blocking Peptide
- Gene:
- SUN2 NIH gene
- Name:
- Sad1 and UNC84 domain containing 2
- Previous symbol:
- UNC84B
- Synonyms:
- -
- Chromosome:
- 22q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-09-13
- Date modifiied:
- 2018-11-19
Related products to: UNC84B Blocking Peptide
Related articles to: UNC84B Blocking Peptide
- Disrupted processing of prelamin A causes Hutchinson-Gilford progeria syndrome (HGPS) and related premature aging disorders. The farnesylated prelamin A variant produced in HGPS, termed progerin, alters actin-nuclear interactions mediated by nesprin-2 and SUN2 LINC complexes resulting in defective cell polarization. To explore further how prelamin A causes these cellular defects, we examined other disease-causing mutations that prevent cleavage of lamin A or reduce the activity of the processing enzyme ZMPSTE24. Accumulation of prelamin A or an uncleaved variant in cells reduced diffusional mobilities of nesprin-2 and SUN2 and inhibited their function in cell polarization in a farnesylation-dependent manner. Expression of short carboxyl-terminal tail fragments of prelamin A variants disrupted cell polarity in a farnesylation-dependent fashion. These results show that retention of the farnesyl moiety in the tails of prelamin A or its variants is the common element responsible for disrupting actin force transmission to the nucleus in premature aging syndromes and support the idea that altered function of actin-dependent LINC complexes is a critical component of premature aging. - Source: PubMed
Publication date: 2026/04/21
Lio ChonkitWang YuexiaWilson Paige CLi YutaoAntoku SusumuÖstlund CeciliaShin Ji-YeonWorman Howard JChang WakamGundersen Gregg G - Microglial dysfunction is a hallmark of Alzheimer's disease (AD), yet the molecular mechanisms driving these impairments remain poorly defined. Genetic studies implicate several AD-associated genes in regulating microglial activity, including SORL1, which encodes the sorting receptor SorLA. Although SorLA is highly expressed in microglia, its functional role in cellular homeostasis has remained unclear. Here, we investigated SorLA function using human brain tissue, primary microglia from rapid autopsies, and CRISPR-engineered human iPSC-derived microglia and neurons. Integrated multi-omics analyses, including single-cell RNA sequencing, lipidomics, and proteomics, together with biochemical and functional assays, revealed that SorLA deficiency induces endoplasmic reticulum (ER) stress and interferon signaling, promotes lipid droplet accumulation, and impairs phagocytic and immune functions. Protein co-complex mapping and structural modeling identified ER-associated proteins co-enriched with SorLA, including SUN2, calnexin (CANX), and multiple COPI complex components (COPA, COPB1, COPG1, ARCN1), implicating SorLA in ER proteostasis and intracellular trafficking. Notably, SORL1 deletion in iPSC-derived neurons recapitulated key phenotypes observed in microglia, including lipid droplet accumulation and SorLA-SUN2 co-immunoprecipitation, indicating that this ER-associated pathway operates across distinct brain cell types. Together, these findings identify an ER-related role for SorLA that extends beyond its established function in endocytic trafficking. Loss of SorLA triggers maladaptive stress responses, perturbs lipid handling, and compromises cellular resilience, thereby contributing to AD-relevant cellular dysfunction. - Source: PubMed
Publication date: 2026/04/06
Haq ImdadulNgo Jason CRoy NainikaLee EmilyChoudhury Muniyat ASoni Rajesh KTeich Andrew FMayeux Richard PDe Jager Philip LHe YeWu XuebingBennett David AOlah MartaSher Falak - Nuclear movement and positioning can be mediated by linker of nucleoskeleton and cytoskeleton (LINC) complexes, which consist of Sad1-UNC-84 (SUN) proteins and Klarsicht-ANC-1-Syne homology (KASH) proteins. KASH proteins bind SUN proteins via a short KASH domain. Unlike animal KASH domains, plant KASH domains are shorter, lack ability to form disulfide bonds and have a different C-terminal sequence motif. Here, we examined the specificity of KASH domains using two Arabidopsis KASH proteins, WIP1 and SINE1. We show experimentally that the SINE1 KASH domain is required for SINE1 function in stomata and the WIP1 KASH domain for WIP1 function in root hairs, but that the SINE1 and WIP1 KASH domains are interchangeable for the WIP1 role in nuclear movement in pollen tubes. Through molecular modeling, we found that SINE1 has two distinct binding modes that are dependent on its interaction partner (SUN1 or SUN2), whereas WIP1 binds very similarly to both SUN1 and SUN2. We propose that this requirement for specific KASH domains reflects differences between the SUN1-SINE1 and SUN1-WIP1 interaction models and might indicate a different tolerance of the interactions to force. - Source: PubMed
Publication date: 2026/04/30
Schumacher Lily AGroves Norman RConway Daniel EMeier Iris - This study aimed to identify centrosome amplification-related genes (CA-RGs) as potential biomarkers in osteoarthritis (OA). - Source: PubMed
Publication date: 2026/02/04
Nie ShixinZhao PeiChen ZhiWu SiyiLi MingxuanLian ChengjieZhang Hua - Fibrosis involves sustained changes in fibroblast gene expression, leading to excessive extracellular matrix (ECM) deposition and progressive tissue stiffening. Although matrix stiffness is a potent regulator of cell fate and transcription, it is not clear how nuclear mechanosensing contributes to fibrosis. Here, we define a central role for SUN2, a component of linker of nucleoskeleton and cytoskeleton (LINC) complexes, as a mediator of stiffness-dependent nuclear and chromatin responses during skin fibrosis. transcripts are upregulated in dermal fibroblasts of patients with systemic sclerosis and Sun2 protein is elevated in fibrotic mouse skin. Nuclear size, A-type lamins and Sun2 are elevated in dermal fibroblasts plated on stiff substrates. Loss of protects against bleomycin-induced skin fibrosis in vivo and abolishes stiffness-induced changes in nuclear size and fibrotic gene expression in vitro. Mechanistically, we identify three -dependent mechanosensitive chromatin states and show that mechanical induction of the histone methyltransferase Ezh2 requires . These findings define SUN2 as a nuclear mechanosensor that couples matrix stiffness to chromatin regulation and transcriptional programs that drive fibrosis, identifying it as a potential therapeutic target pathway in fibrotic disease. - Source: PubMed
Publication date: 2026/03/20
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