ADRM1
- Known as:
- ADRM1
- Catalog number:
- 001249A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ADRM1
Related genes to: ADRM1
- Gene:
- ADRM1 NIH gene
- Name:
- adhesion regulating molecule 1
- Previous symbol:
- -
- Synonyms:
- GP110, Rpn13, ARM1
- Chromosome:
- 20q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-17
- Date modifiied:
- 2015-09-11
Related products to: ADRM1
Related articles to: ADRM1
- Sperm capacitation is a complex process that induces biological and biochemical changes in spermatozoa, leading to successful oocyte fertilisation. In this study, we investigated the role of the ubiquitin-proteasome system (UPS) in the remodelling of proteasomal subunits during in vitro capacitation of bovine spermatozoa. We selectively separated proteins from non-capacitated and in vitro-capacitated (IVC) bovine spermatozoa and analysed the purified proteins using four liquid chromatography-mass spectrometry (LC-MS) replicates. This analysis indicated the downregulation of 26S proteasome components, specifically the proteasome 26S subunit, non-ATPase 1 (PSMD1), and adhesion regulating molecule 1 (ADRM1), during bovine spermatozoa capacitation. Immunofluorescence localisation, image-based flow cytometry, and western blotting were used to demonstrate changes in PSMD1, ADRM1, and ubiquitination (UB) during in vitro capacitation. The results showed a significant increase in protein tyrosine phosphorylation and ubiquitination levels, along with a significant decrease in PSMD1 and ADRM1 expression. The binding levels of ADRM1 to PSMD1 and UB were also significantly enhanced. Additionally, inhibiting ADRM1 binding to PSMD1 resulted in significant increases in PSMD1 and ADRM1 expression, and a significant decrease in ADRM1 binding to UB. These findings confirmed that the UPS plays a role in proteasomal subunit changes during bovine sperm capacitation. - Source: PubMed
Publication date: 2026/05/02
Cao LipengLi ChunyuHan YueLv YanqiuWang JieQu XinglinZhang YuyangGu WeiyuXu QinglongYao ShunfaLu JinweiLv AihuiChen XuanJin Yi - The 26S proteasome typically degrades proteins marked by ubiquitin chains. However, a distinct, ubiquitin-independent degradation pathway for nuclear proteins exists, mediated by the adaptor protein midnolin, yet its molecular mechanism remains poorly understood. Here, we present nine cryo-electron microscopy structures of the human 26S proteasome in complex with midnolin, which collectively delineate a near-complete catalytic cycle. Our structures reveal that midnolin binds to the proteasome via the RPN1 subunit by its C-terminal helix. Unexpectedly, its ubiquitin-like domain interacts with the RPN11 deubiquitinase in a non-catalytic role. This interaction positions the adjacent Catch domain, which is responsible for substrate binding, directly above the proteasomal entrance, potentially facilitating substrate entry into the proteasome. Furthermore, we observe four consecutive spiral staircase conformations of the AAA+ ATPase hexamer during substrate translocation. These findings provide insights into the mechanisms underlying ubiquitin-independent nuclear protein degradation and may help develop strategies for targeting nuclear proteins via direct proteasomal degradation. - Source: PubMed
Publication date: 2026/03/27
Zhu ChuandaQin LuDai ZonglinZuo PengYang AoZhong LijunLin ZhiqiangLiang Ling - Adhesion regulating molecule 1 (ADRM1), also known as regulatory particle non-ATPase subunit 13 (Rpn13), is a multifunctional proteasome-associated ubiquitin receptor that bridges protein degradation and cellular signaling networks. Structurally, ADRM1 comprises an N-terminal pleckstrin-like receptor for ubiquitin (Pru) domain responsible for ubiquitin and proteasome recognition, and a C-terminal DEUBAD domain that activates the deubiquitinating enzyme UCH37, jointly coordinating substrate recognition and deubiquitination within the 26S proteasome. Functionally, ADRM1 regulates multiple biological processes including cell adhesion, cytoskeletal remodeling, and signaling transduction. By interacting with Phg2, HDAC8, and PADI4, ADRM1 modulates cytoskeletal homeostasis and cell motility through transcriptional and post-translational mechanisms. Overexpression of ADRM1 has been consistently observed in a wide spectrum of malignancies such as colorectal, ovarian, gastric, hepatic, and multiple myeloma where it promotes tumor proliferation, migration, metastasis, and therapeutic resistance, underscoring its oncogenic potential. In addition to its cancer-related functions, ADRM1 plays crucial roles in bone metabolism, reproductive development, and immune regulation. It modulates osteoblast and osteoclast differentiation via the RANKL/OPG axis and participates in gametogenesis and endocrine balance, revealing its systemic physiological importance. Recent advances in structural biology, gene editing, and proteomic technologies have significantly deepened the mechanistic understanding of ADRM1 and facilitated the identification of small-molecule inhibitors such as RA190, which selectively target its Pru domain and exhibit strong anti-tumor efficacy. Collectively, ADRM1 represents a pivotal molecular hub integrating proteasomal activity with diverse signaling networks and holds promise as a diagnostic biomarker and therapeutic target across multiple disease contexts. - Source: PubMed
Publication date: 2026/03/09
Chen YimingXu TiantianZhou TonghuaShan JingZhu Meisong - Kidney renal clear cell carcinoma (KIRC), as the major type of renal cell carcinoma, remains challenging due to its rapid malignant progression and poor prognosis. Adhesion-regulating molecule 1 (ADRM1) has been implicated in tumor development, yet its specific role in KIRC is poorly understood. - Source: PubMed
Publication date: 2025/12/09
Li LikunWang LiminCao DongxiaLi XiaoruGe MuyaYuan YeSong Bo - Atherosclerosis accelerates the progression of diabetes and metabolic syndrome. Endothelial to mesenchymal transition (EndMT) has been reported to promote the development of atherosclerosis and the generation of extracellular matrix. However, the mechanism of EndMT in diabetic atherosclerosis has not been fully clarified. - Source: PubMed
Zhang ZhiwenGuo QuanZhao ZhenzhouNie MingShi QingboLi EnLiu KaiyuanYu HaosenRao LixinLi Muwei