UNC84B Blocking Peptide
- Known as:
- UNC84B Blocking Peptide
- Catalog number:
- 33r-8772
- 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
- Vascular endothelial cells respond to environmental forces to remodel vessels during development and to achieve homeostasis, and mis-regulated responses lead to vascular dysfunction and disease. The nucleus participates in force transduction to cell-matrix junctions via the Linker of Nucleoskeleton and Cytoskeleton (LINC) complex that resides in the nuclear envelope, but how these forces are regulated and relayed is incompletely understood. We found that the LINC complex protein SUN2 is required for proper endothelial cell-matrix interactions that occur far from the nucleus and affect angiogenic expansion, vascular responses to flow, and barrier integrity. Endothelial cells lacking SUN2 had inappropriate flow responses and reduced expression of flow-mediated transcription factors and . Expression of several matrix and adhesion genes was reduced in SUN2-depleted cells, leading to defective extracellular matrix, dysmorphic focal adhesions resistant to dynamic turnover, and disturbed cell-matrix force distribution. Mechanistically, nuclear SUN2 affected dynamic regulation of the microtubule cytoskeleton that correlated with matrix metalloprotease-dependent barrier dysfunction. These findings indicate that nuclear SUN2 establishes and maintains blood vessel homeostasis by controlling microtubule-mediated effects on focal adhesion turnover and extracellular matrix properties, with implications for cardiovascular aging and diseases such as Marfan syndrome that affect vessel wall integrity. - Source: PubMed
Publication date: 2026/05/20
Bougaran PaulineBuglak Danielle BNeal AlexandraRathod MiteshGore MichaelanthonyHockenberry Max AAmin Aryan ATanke NatalieOatley MorganLegant Wesley RLiu ZiqingBear James EPolacheck William JBautch Victoria L - SUN1/2, core components of the linker of nucleoskeleton and cytoskeleton complex, transmit extracellular mechanical forces to nuclear lamina and chromatin. However, their role in regulating peripheral chromatin in mechanosensing and mechanoadaptation remains unclear. Using CRISPR/Cas9-mediated knockout of or in myoblasts, we identified a SUN1/2-dependent mechano-feedback loop. SUN1/2 depletion down-regulates genes for cell adhesion (e.g., integrin alpha-4) and for mechanotransduction (e.g., cell division cycle 42 and Ras homolog family member A). The primary mechanism involves redistribution of heterochromatin from nuclear periphery to the nucleoplasm and remodeling of lamina-associated domains (LADs), as an adaptive response to the loss of SUN proteins. Furthermore, lamin A/C acts as a key downstream effector, consistently modulating adhesion-related gene expression through the remodeling of LADs. Functionally, knockout of either or aggravates differentiation defects in C2C12 myoblasts and abolishes adaptive responses to mechanical cues. This study provides proof of concept that nuclear mechanotransduction proteins can modulate cellular mechanoadaptation via a mechano-feedback loop, which coordinates LAD reorganization with the expression of upstream mechanotransduction genes. - Source: PubMed
Publication date: 2026/05/14
Xie YafanZuo ZhaoyanLu ChenfeiZhao YanjingGuo LipingXu WeiLiu FuhaiGuidoin RobertZhang HaoyueQiu JuhuiWang GuixuePeng Qin - Heart specialization involves nuclear programs; however, chamber-specific regulation of the nuclear proteome landscape remains unknown. In this study, we isolated the nucleus from four major anatomical regions of healthy mouse heart (fresh) and employed quantitative mass spectrometry-based proteomics to construct a comprehensive nuclear proteome landscape of left ventricle (LV, 2403 proteins), right ventricle (RV, 2242 proteins), left atrium (LA, 2368 proteins), and right atrium (RA, 1816 proteins). This led to the discovery of nuclear regional proteome signatures (ventricular signature, 297 proteins; atrial signature, 183 proteins) associated with oxidative metabolism and redox regulation, ferroptosis, extracellular-matrix remodeling, SUMO- and stress-responsive control and transcriptional regulation. Chamber-level analyses further identify distinct nuclear features in LV (120 proteins), LA (188 proteins), and RA (72 proteins). In addition, we defined conserved core nuclear proteome (230 proteins) shared across all anatomical regions, enriched for transcription-regulator complexes, nucleolar/ribosome-associated, RNA-processing, and chromatin-organization components. Within this core network, we report 78 transcription factors/co-factors and select nuclear, chromatin and RNA export-associated proteins, including 29 specific factors (e.g., Alpk3, Rbm14, Arglu1, Hmgb1, Myef2, Sf1) associated with the heart. Regionally, we verified spatial localization in heart of H2ac21 and Sun2 in LA and Ptbp2 in LV by immunofluorescence. This study provides insights into the chamber-resolved view of the nuclear proteome in the heart, establishes a framework for linking nuclear proteomic signatures to atrial and ventricular biology, unique features of the heart nuclear proteome landscape relative to other organs, and a baseline for studying nuclear remodeling in cardiac pathophysiology. - Source: PubMed
Publication date: 2026/05/14
Eslami Seyed SadeghRai AlinFang HaoyunThomas AnitaCross JonathonDonner DanielGreening David W - Disrupted processing of prelamin A (encoded by LMNA) 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 linker of nucleoskeleton and cytoskeleton (LINC) complexes, resulting in defective cell polarization. To explore further how prelamin A causes these cellular defects, we examined other disease-causing variants 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: 2026/05/18
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