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
- Hereditary spastic paraplegia (HSP) comprises a heterogeneous group of inherited neurodegenerative disorders characterized by progressive spasticity and weakness primarily of the lower extremities. Data describing pediatric HSP from the Levant region remain limited. - Source: PubMed
Publication date: 2026/07/14
Habanjar DimaKreidly SihamTrad SamahBoustany Rose-Mary - Hypertrophic olivary degeneration (HOD) is a rare form of transsynaptic degeneration resulting from disruption of the Guillain-Mollaret triangle, typically presenting with palatal tremor, ataxia, and nystagmus. Mutations in the Ring Finger Protein 170 (RNF170) gene have been associated with autosomal dominant sensory ataxia. However, the coexistence of HOD and an RNF170 mutation has rarely been reported. A 60-year-old female presented with progressive gait instability, vertigo, oscillopsia, and a sensation of walking on cotton. Neurological examination revealed pendular nystagmus, slow rhythmic palatal myoclonus, broad-based gait, positive Romberg sign, and clumsy tandem gait. Cognitive function was intact. Magnetic resonance imaging showed bilateral hypertrophy of the inferior olivary nuclei with T2 hyperintensity, consistent with HOD, along with mild right cerebellar atrophy. No brainstem infarction, hemorrhage, or demyelinating lesions were identified. Genetic testing revealed a heterozygous mutation in the RNF170 gene. There was no family history of ataxia, and screening for common spinocerebellar ataxia genes was negative. This case describes an unusual presentation of HOD without an identifiable secondary structural lesion, occurring in a patient with an RNF170 mutation. The findings suggest that RNF170-related neurodegeneration may predispose to or mimic HOD. In patients with unexplained HOD and prominent ataxia, screening for RNF170 gene mutations should be considered. - Source: PubMed
Publication date: 2026/04/26
Wang Change - The endoplasmic reticulum 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-electron microscopy, we determined the structures of the Erlin1-Erlin2 complex, the Erlin1-Erlin2-RNF170 complex, and the 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
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