Ask about this productRelated genes to: RNF170 antibody
- Gene:
- RNF170 NIH gene
- Name:
- ring finger protein 170
- Previous symbol:
- SNAX1
- Synonyms:
- DKFZP564A022, ADSA
- Chromosome:
- 8p11.21
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-26
- Date modifiied:
- 2016-11-01
Related products to: RNF170 antibody
Related articles to: RNF170 antibody
- The endoplasmic reticulum (ER) lipid raft proteins (Erlins) belong to the stomatin-prohibitin-flotillin-HflC/K (SPFH) family and form highly oligomeric platforms that mediate the degradation of activated inositol 1,4,5-trisphosphate receptors by facilitating their interaction with the E3 ligase RNF170. However, the molecular mechanisms underlying this process remain unclear. Here, we successfully reconstituted the Erlin1-Erlin2 complex and its complex with RNF170 by overexpressing these components in HEK293F cells. We also isolated the Erlin2 oligomer by solely expressing Erlin2 in the cells. Using cryo-EM, we determined the structures of the Erlin1-Erlin2 complex, Erlin1-Erlin2-RNF170 complex, and Erlin2 oligomer at resolutions of 3.29 Å, 3.05 Å, and 2.12 Å, respectively. Both the Erlin1-Erlin2 complex and the Erlin2 oligomer exhibit similar cage-like architectures, with the Erlin1-Erlin2 complex containing 13 pairs of Erlin1 and Erlin2 subunits, whereas the Erlin2 oligomer comprises 26 Erlin2. Although RNF170 was clearly identified during protein purification, it was invisible in the final 3D reconstruction, suggesting a high degree of flexibility between RNF170 and the Erlin complex. Multiple water molecules were identified in the Erlin2 oligomer, underscoring their critical roles in facilitating the high degree of oligomerization of the Erlin2 complex. Taken together, our structural investigation elucidates the molecular basis for the assembly of the Erlin complex and provides a framework for further investigation. - Source: PubMed
Publication date: 2026/01/02
Jia XiaoxiaoLiu GuoyunLi HaiwenQian Hongwu - Sensory ataxic neuropathies (SAN) are rare large fibre sensory neuropathies characterised by progressive sensory loss and ataxia. They may be inherited or acquired. When inherited they are more commonly seen as part of a broader syndrome involving cerebellar ataxia or mitochondrial dysfunction. Isolated inherited SAN are rare, and the causes are limited, including RFC1 expansions (CANVAS), POLG variants and variants in COX20 and RNF170. Spinocerebellar ataxia type 15 (SCA15), caused by deletions in the ITPR1 gene, is another potential genetic cause of SAN, as peripheral neuropathy is commonly associated with various spinocerebellar ataxias. - Source: PubMed
Haddad SaifPoh RoyHehir JasonPolke James MBlake JulianReilly Mary M - Endoplasmic reticulum lipid raft-associated protein 1 (ERLIN1) is an endoplasmic reticulum (ER)-resident stomatin/prohibitin/flotillin/HflK/C (SPFH) family protein that assembles into oligomeric complexes within detergent-resistant membrane domains. ERLIN1 regulates multiple cellular functions, including protein quality control, calcium signaling, and lipid metabolism. Together with ERLIN2, it forms ER-associated degradation (ERAD) nanodomains through interactions with RING finger protein 170 (RNF170) and transmembrane and ubiquitin-like domain-containing 1 (TMUB1). These specialized domains facilitate the degradation of inositol 1,4,5-trisphosphate receptor type 1 (IP3R) via the ERAD pathway. ERLIN1 also controls cholesterol metabolism by inhibiting sterol regulatory element-binding protein (SREBP) activation and promoting 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) degradation. In addition, it blocks cholesterol esterification, thereby enhancing cholesterol transport to the Golgi apparatus. ERLIN1 further regulates cell fate by promoting autophagy and suppressing apoptosis; in complex with ERLIN2, it interacts with activating molecule in Beclin 1-regulated autophagy protein 1 (AMBRA1) at mitochondria-associated membranes to initiate autophagy and binds phosphatidylinositol 3-phosphate to stabilize autophagy signaling. Its overexpression enhances tumor progression, whereas silencing triggers apoptosis in colorectal cancer. Mutations in ERLIN1 are linked to neurodegenerative diseases such as hereditary spastic paraplegia type 62 and atypical amyotrophic lateral sclerosis. The ERLIN1/2 complex also influences immune responses and viral replication through cholesterol regulation. Collectively, these diverse and integrated functions highlight the potential of ERLIN1 as a therapeutic target in cancer, metabolic, neurodegenerative, and infectious diseases. - Source: PubMed
Publication date: 2025/11/06
Cho HyojeongLee BeomwooSon ChanggyuChoi JaeseokEom SunhoPark Jongsun - We investigated the mechanism by which eupalinolide B (EB) regulates DEK protein ubiquitination and degradation, and its impact on DEK-mediated receptor-interacting protein kinase 1 (RIPK)-PANoptosis pathway in allergic asthma. - Source: PubMed
Publication date: 2025/03/17
Bai QiaoyunWang ChongyangDing NingpoWang ZhiguangLiu RuobaiLi LiangchangPiao HongmeiSong YilanYan Guanghai - - Source: PubMed
Publication date: 2024/12/08