Ask about this productRelated genes to: ANXA11 antibody
- Gene:
- ANXA11 NIH gene
- Name:
- annexin A11
- Previous symbol:
- ANX11
- Synonyms:
- -
- Chromosome:
- 10q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-05-17
- Date modifiied:
- 2014-11-19
Related products to: ANXA11 antibody
Related articles to: ANXA11 antibody
- Amyotrophic Lateral Sclerosis (ALS) is a fatal neurodegenerative disease marked by progressive motor neuron loss, leading to muscle paralysis and respiratory failure. Genetic mutations, notably in the ANXA11 gene, have been implicated in both familial and sporadic ALS forms. ANXA11 functions as a cellular "tether," orchestrating the transport of RNA-protein complexes and lysosomes through its N-terminal (Nt) and C-terminal (Ct) domains, respectively. This study uncovers a novel calcium-dependent regulatory mechanism governing the intramolecular interaction between these domains. Using biochemical, biophysical, and computational approaches, we suggest that in the absence of calcium, ANXA11 adopts a closed conformation with stable Nt-Ct interactions. Elevated calcium levels induce a conformational shift, disrupting this interaction and exposing binding sites for RNA and membranes. Crucially, we show that the ALS-associated D40G mutation in the Nt domain impairs this calcium-regulated interaction, favoring a persistent open conformation that predisposes to toxic protein aggregation. These findings reveal that calcium acts as a molecular switch modulating ANXA11 conformation and function, providing new insights into its role in ALS pathogenesis and potential therapeutic targets. - Source: PubMed
Publication date: 2026/03/28
Di Napoli GiuliaAlfurno LorenzoFissore AlexRaccuia EleonoraOlivieri PaoloMarengo MauroOliaro-Bosso SimonettaPiaz Fabrizio DalCatucci GianlucaGilardi GianfrancoVelazquez-Campoy AdrianPrischi FilippoDe Simone AngelaSpyrakis FrancescaDi Palma FrancescoAdinolfi Salvatore - Frontotemporal lobar degeneration TDP43 type C (TDP-C) is a rare and unique neurodegenerative disease that attacks the anterior temporal lobe. Recently, it was shown that Annexin-A11 and TDP-43 coaggregate specifically in TDP-C. Current literature on the genetic associations with TDP-C, reviewed here, lacks a discernible corpus of robust or replicated findings. In this study, using blood tissue, we completed whole genome sequencing to investigate and genetic variants for their association with TDP-C. Then, we completed genome-wide hypothesis-free analyses using artificial intelligence to identify rare pathogenic variants associated with TDP-C. - Source: PubMed
Publication date: 2026/03/23
Nassan MalikAyala IvanSloan JenniferBonfitto AnnaStark BobbiSong SerenaNaymik MarcusGeula ChangizGefen TamarBarbieri ElenaPiras IgnazioMesulam M-MarselHuentelman Matthew - Pelizaeus-Merzbacher disease (PMD) is a devastating, X-linked hypomyelinating leukodystrophy caused by mutations in a myelin gene, PLP1. While overwhelming endoplasmic reticulum (ER) stress caused by the accumulation of mutant PLP1 is widely recognized, blockade of the apoptotic arm of the unfolded protein response (UPR) failed to rescue the phenotypes in murine disease models, suggesting the involvement of additional, critical cellular mechanisms in oligodendrocyte dysfunction. Herein, we identified ER Ca depletion and disrupted ER-Golgi trafficking as key cellular pathologies in PMD. Mutant PLP1 impairs COPII vesicle formation by destabilizing its key components, including Sec31A at ER exit sites due to the Ca transport dysregulation and deconstruction of the ALG-2/Sec31A/AnxA11 interaction. Pharmacological restoration of ER Ca levels rescued COPII formation. These findings highlight how PLP1 mutations affect the intracellular trafficking of membrane and secretory proteins through the ER Ca depletion, which may be associated with the clinical consequences of PMD and other inherited myelin disorders. - Source: PubMed
Publication date: 2026/02/24
Li HengMishima ReikoGoto Yu-IchiInoue Ken - Multisystem proteinopathy (MSP) is a pleiotropic group of disorders initially presenting as inclusion body myopathy (IBM), amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and/or Paget disease of bone (PDB). Additional genes including , and , have recently been implicated in MSP-like disorders, further expanding the genetic spectrum. This research aims to study the genetic and clinical characteristics of MSP and related disorders in a large Chinese cohort. - Source: PubMed
Publication date: 2026/02/18
Xia XingyuChen XiSun YimingZhang MingQiao KaiChen YanZhao ChongboDong YiZhu Wenhua - Aberrant protein aggregation is a hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), which share overlapping genetic and pathological features. Similar aggregates are increasingly recognized in Alzheimer's disease (AD) and limbic-predominant age-related TDP-43 encephalopathy (LATE). However, it remains unclear whether a shared molecular pathway drives this pathological aggregation. Here, we report that the E3 ubiquitin ligase TRIM32, together with the shuttle factor UBQLN2 and the autophagy adaptor p62/SQSTM1, form condensates that depend on E3 ligase activity and a network of intermolecular interactions. These condensates act as scaffolds that capture UBQLN2 client proteins, including TDP-43 and ANXA11, and modulate their mobility. A unique hydrophobic loop within TRIM32's substrate-binding domain mimics low-complexity motifs in ANXA11 and TDP-43, enabling selective retention via competitive binding mediated by UBQLN2 STI1 domain. Moreover, TRIM32 condensates promote amyloid aggregation of TDP-43, an effect that is exacerbated by pathogenic UBQLN2 mutation. In brains from individuals with diverse neurodegenerative diseases, TRIM32 co-localizes with pathological phospho-TDP-43 (pTDP-43) inclusions, supporting a model in which TRIM32-driven condensates function as selective proteostasis sorting compartments that broadly contribute to TDP-43 proteinopathy. - Source: PubMed
Publication date: 2026/02/13
He ZiyanZhou JiechaoZhang RongzhenMeng FeiNauen David WTroncoso Juan CWorley Paul FZhang Wenchi