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ProteomicsThe ER-phagy receptor FAM134B is targeted by Salmonella Typhimurium to promote infection
Macroautophagy/autophagy is a key catabolic-recycling pathway that can selectively target damaged organelles or invading pathogens for degradation. The selective autophagic degradation of the endoplasmic reticulum (hereafter referred to as ER-phagy) is a homeostatic mechanism, controlling ER size, t...
ORGANISM(S): Homo sapiens (Human) Salmonella enterica subsp. enterica 
2025-05-07 | PXD061148 | Pride
Ap-ms sopf fam134b 
ProteomicsFAM134B oligomerization drives ER membrane scission for ER-phagy
ER degradation by selective autophagy (ER-phagy) is crucial for ER homeostasis. However, it remains unclear how ER scission is regulated for subsequent autophagosomal sequestration and lysosomal degradation. Here, we show that oligomer formation of FAM134B (also referred to as reticulophagy regulato...
ORGANISM(S): Homo sapiens (Human) 
2020-01-09 | PXD016661 | Pride
Er-phagy  fam134b oligomerization  membrane fragmentation  er stress  camk2b 
ProteomicsFAM134B homodimer ubiquitination
FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032740 | Pride
Venus fam134b and fam134c dimers 
GenomicsFAM134B deficiency in HK-2 cells
FAM134B deficiency in HK-2 cells
PRJNA1141991 | ENA
ProteomicsUbiquitination promotes FAM134B-mediated ER-phagy
FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032721 | Pride
Gfp-fam134b Ubiquitin 
ProteomicsE3 ligase regulates FAM134B ubiquitination
FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032750 | Pride
Venus amfr fam134b basal torin1 
ProteomicsFAM134B oligomer ubiquitination and ER-phagy
FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032741 | Pride
Venus fam134b ubiquitinated sites 
ProteomicsBinding partners of FAM134B WT and 17KR oligomers
FAM134B is a reticulon-homology domain (RHD)-containing protein that participates in membrane-shaping of the endoplasmic reticulum (ER)8 13. It also functions as a mammalian ER-phagy receptor, mediating the fragmentation and selective degradation of ER sheets in multiple cell types8. However, little...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032743 | Pride
Venus fam134b wt and 17 kr 
TranscriptomicsFAM134B deficiency in HK-2 cells
FAM134B, also known as RETREG1 or JK-1, was first identified in esophageal cancer and later identified as an ER autophagy receptor. The protein contains a Reticulon-homology domain(RHD) and an LC3 interaction region (LIR), where RHD is responsible for sensing and inducing ER membrane curvature, whil...
ORGANISM(S): Homo sapiens 
2025-07-31 | GSE273481 | GEO
ProteomicsARL6IP1 and FAM134B forms a complex
ER-resident membrane-shaping proteins with central reticulon homology domains (RHDs) have been associated with neurodegenerative disorders such as ARL6IP1 and FAM134B.Mutations in ARL6IP1 cause SPG61, a neurodegenerative disorder characterized by progressive leg spasticity (hereditary spastic parapl...
ORGANISM(S): Homo sapiens (Human) 
2023-06-19 | PXD032720 | Pride
Venus arl6ip1 and heterodimer fam134b 
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