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ProteomicsTranscriptional regulation of FAM134B by TFEB/TFE3 controls ER-phagy in response to starvation and chondrocyte differentiation
Lysosomal degradation of the endoplasmic reticulum (ER) via autophagy (ER-phagy) is emerging as a critical regulator of cell homeostasis and function1. The recent identification of ER-phagy receptors has shed light on the molecular mechanism underlining this process; however, the signaling pathways ...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-07-15 | PXD015326 | Pride
Lysosome Tfeb Er-phagy Chondrocyte 
ProteomicsTranscriptional regulation of ER-phagy by MiT/TFE factors controls chondrocyte differentiation and bone formation
Lysosomal-autophagic degradation of Endoplasmic Reticulum via autophagy (ER-phagy) is emerging as critical regulator of ER homeostasis and function. However, the molecular mechanisms governing ER-phagy are still unknown. Working in chondrocytes, we found that ER-phagy and lysosome biogenesis are co-...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-07-15 | PXD015331 | Pride
Phosphoprotemics Fgf signaling Er-phagy 
ProteomicsAn mTORC1-CK2 axis controls starvation induced ER-phagy via FAM134C
The degradation of endoplasmic reticulum (ER) via selective autophagy is driven by the ER-phagy receptors that facilitate the incorporation of ER-fragments into nascent autophagosomes. How these receptors are regulated, in response to ER-phagy-inducing stimuluses, is largely unknown. Here we propose...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2022-10-14 | PXD030451 | Pride
Human Fam134c Autophagy Rat Ck2 Mtorc1 Er-phagy 
ProteomicsMiT/TFE factors control ER-phagy via transcriptional regulation of FAM134B
Lysosomal degradation of the endoplasmic reticulum (ER) via autophagy (ER-phagy) is emerging as a critical regulator of ER homeostasis and function1. The selective incorporation of ER fragments into nascent autophagosomes is facilitated by ER resident proteins, ER-phagy receptors, that bind the auto...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-07-15 | PXD015130 | Pride
Erphagy secretome 
ProteomicsArylsulfatase L (ARSL) Controls Glycosaminoglycan Sulfation During Skeletal Development
Proteoglycans are essential components of the cartilage extracellular matrix (ECM), with glycosaminoglycan (GAG) chains playing a crucial role in skeletal development. This study identifies a previously unknown substrate of arylsulfatase L (ARSL) a Golgi-localized enzyme. To investigate ARSL’s physi...
ORGANISM(S): Rattus norvegicus (Rat) 
2026-06-15 | PXD061172 | Pride
Arsl Skeletal Glycosaminoglycan 
TranscriptomicsDIRECT CONVERSION OF FIBROBLASTS INTO FUNCTIONAL ASTROCYTES BY DEFINED TRANSCRIPTION FACTORS
Direct cell reprogramming has enabled the direct conversion of skin fibroblasts into functional neurons and oligodendrocytes using a minimal set of cell lineage-specific transcription factors. This approach has substantial advantages since it is rapid and simple, generating the cell type of interest...
ORGANISM(S): Mus musculus 
2015-06-22 | E-GEOD-59018 | biostudies-arrayexpress
ProteomicsCritical functions of FAM134 family members in endoplasmic reticulum remodeling, ER-phagy and collagen quality control
Degradation of the endoplasmic reticulum (ER) by selective autophagy (ER-phagy) is vital for cellular homeostasis. Here, we introduce FAM134A/RETREG2 and FAM134C/RETREG3 as new ER-phagy receptors. FAM134A and FAM134C exist in a relatively inactive state under basal conditions and require an activati...
ORGANISM(S): Homo sapiens (Human) 
2021-06-23 | PXD025626 | Pride
Collagen Fam134 Endoplasmic reticulum Er-phagy Retreg Autophagy U2os. 
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