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Binding partners of FAM134B WT and 17KR oligomers

ABSTRACT: 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 is known about the molecular and biophysical mechanisms that control and/or switch between these two FAM134B functions.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Adriana Covarrubias-Pinto

LAB HEAD: Ivan Dikic

PROVIDER: PXD032743 | Pride | 2023-06-19

REPOSITORIES: Pride

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			Action	DRS
	20210426_Venus_Empty_01.raw	Raw
	20210426_Venus_Empty_02.raw	Raw
	20210426_Venus_Empty_03.raw	Raw
	20210426_Venus_FAM134B_17KR_control_01.raw	Raw
	20210426_Venus_FAM134B_17KR_control_02.raw	Raw

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FAM134B homodimer ubiquitination

Project description: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 is known about the molecular and biophysical mechanisms that control and/or switch between these two FAM134B functions.

2023-06-19 | PXD032740 | Pride

FAM134B oligomer ubiquitination and ER-phagy

2023-06-19 | PXD032741 | Pride

E3 ligase regulates FAM134B ubiquitination

2023-06-19 | PXD032750 | Pride

Ubiquitination promotes FAM134B-mediated ER-phagy

2023-06-19 | PXD032721 | Pride

ARL6IP1 is an interacting partner of the ER-phagy receptor FAM134B

Project description: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 paraplegia/HSP) in combination with loss of sensory and pain perception, thus reproducing typical symptoms of HSAN {Kurth, 2009 #8;Novarino, 2014 #28;Nizon, 2018 #162}.Our objetive was to analyse FAM134B-ARL6IP1 protein protein interactionS to underlying mechanisms, required for effective ER-remodelling and ER-phagy.

2023-06-19 | PXD032718 | Pride

ARL6IP1 and FAM134B forms a complex

2023-06-19 | PXD032720 | Pride

E3 ligase AMFR regulates ARL6IP1 Ubiquitination in cells

2023-06-19 | PXD039184 | Pride

The function of ER-phagy receptors is regulated through phosphorylation-dependent ubiquitination pathways.

Project description:Selective autophagy of the endoplasmic reticulum (ER), known as ER-phagy, is an important regulator of ER remodeling and is critical to maintaining cellular homeostasis during environmental changes. We recently showed that members of the FAM134 family play a role during stress-induced ER-phagy. However, the mechanisms on how they are activated remain largely unknown. In this study, we analyzed mTOR-mediated phosphorylation of FAM134 as a trigger of FAM134-driven ER-phagy. An unbiased screen of kinase inhibitors revealed that CK2 is essential for ER-phagy driven by FAM134B and FAM134C after inhibition of mTOR. Using superresolution microscopy, we showed that CK2 activity is essential for the formation of high-density groups of FAM134B and FAM134C. Continually, the FAM134B and FAM134C proteins that carry point mutations of selected serine residues within their reticulon homology domain are unable to form high-density clusters. Furthermore, we provide evidence that ubiquitination regulates ER-phagy receptors and that dense clustering of FAM134B and FAM134C requires events upstream of ubiquitination. Treatment with the CK2 inhibitor SGC-CK2-1 or mutation of phosphosites prevents Torin1-induced ER-phagy flux as well as ubiquitination of FAM134 proteins, and consistently treatment with E1 inhibitor suppresses Torin1-induced ER-phagy flux. Therefore, we propose that CK2 dependent phosphorylation of ER-phagy receptors precedes ubiquitin-dependent activation of ER-phagy flux.

2023-11-16 | PXD043003 | Pride

In vivo FAM134B ubiquitination in AMFR KD cells

2023-06-19 | PXD039187 | Pride

The ER-phagy receptor FAM134B is targeted by Salmonella Typhimurium to promote infection

Project description: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, the removal of misfolded protein aggregates, and organelle damage. ER-phagy can also be stimulated by pathogen infection. However, the link between ER-phagy and bacterial infection remains poorly understood, as are the mechanisms evolved by pathogens to escape the effects of ER-phagy. Here, we show that Salmonella enterica serovar Typhimurium inhibits ER-phagy by targeting the ER-phagy receptor FAM134B, leading to a pronounced increase in Salmonella burden after invasion. Salmonella prevents FAM134B oligomerization, which is required for efficient ER-phagy. FAM134B knock-out raises intracellular Salmonella number, while FAM134B activation reduces Salmonella burden. Additionally, we found that Salmonella targets FAM134B through the bacterial effector SopF to enhance intracellular survival through ER-phagy inhibition. Furthermore, FAM134B knock-out mice infected with Salmonella presented severe intestinal damage and increased bacterial burden. These results provide mechanistic insight into the interplay between ER-phagy and bacterial infection, highlighting a key role for FAM134B in innate immunity.

2025-05-07 | PXD061148 | Pride

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