Peroxisomal Membrane Contact Sites in Mammalian Cells

Chen, Chao; Li, Jing; Qin, Xuhui; Wang, Wei

doi:10.3389/fcell.2020.00512

Cited by 22 publications

(18 citation statements)

References 91 publications

(118 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As a cytoskeletal protein, SPTN1 is known to be involved in stabilization of the plasma membrane and to organize intracellular organelles [ 164 ]. These data corroborate the existence of peroxisome interconnection with LDs and the cytoskeleton [ 165 , 166 ].…”

Section: Protein Interactions and Unexpected Rolessupporting

confidence: 86%

“…Since peroxisomal lipid metabolism requires cooperation and interaction with mitochondria, ER and LDs, peroxisomal ABC transporters, through their interactome, could therefore actively participate in this intracellular metabolic network. Peroxisome-organelle interactions have physiological relevance [ 166 , 173 ], and peroxisomes are increasingly considered important intracellular signaling platforms that modulate physiological processes such as inflammation, innate immunity and cell fate decision [ 12 , 174 , 175 ]. Peroxisomal ABC transporters would play an essential part in this emerging role of peroxisomes in signaling pathways such as calcium signaling as highlighted in this review.…”

Section: Protein Interactions and Unexpected Rolesmentioning

confidence: 99%

See 1 more Smart Citation

Peroxisomal ABC Transporters: An Update

Tawbeh

Gondcaille

Trompier

et al. 2021

IJMS

View full text Add to dashboard Cite

ATP-binding cassette (ABC) transporters constitute one of the largest superfamilies of conserved proteins from bacteria to mammals. In humans, three members of this family are expressed in the peroxisomal membrane and belong to the subfamily D: ABCD1 (ALDP), ABCD2 (ALDRP), and ABCD3 (PMP70). These half-transporters must dimerize to form a functional transporter, but they are thought to exist primarily as tetramers. They possess overlapping but specific substrate specificity, allowing the transport of various lipids into the peroxisomal matrix. The defects of ABCD1 and ABCD3 are responsible for two genetic disorders called X-linked adrenoleukodystrophy and congenital bile acid synthesis defect 5, respectively. In addition to their role in peroxisome metabolism, it has recently been proposed that peroxisomal ABC transporters participate in cell signaling and cell control, particularly in cancer. This review presents an overview of the knowledge on the structure, function, and mechanisms involving these proteins and their link to pathologies. We summarize the different in vitro and in vivo models existing across the species to study peroxisomal ABC transporters and the consequences of their defects. Finally, an overview of the known and possible interactome involving these proteins, which reveal putative and unexpected new functions, is shown and discussed.

show abstract

Section: Protein Interactions and Unexpected Rolessupporting

confidence: 86%

Section: Protein Interactions and Unexpected Rolesmentioning

confidence: 99%

Peroxisomal ABC Transporters: An Update

Tawbeh

Gondcaille

Trompier

et al. 2021

IJMS

View full text Add to dashboard Cite

show abstract

“…Interestingly, the peroxisomal protease did induce mild HiLITR activation with the mitochondrial TF ( G ). This may be due to mitochondria-peroxisome contact sites ( Chen et al, 2020 ), which could produce crosstalk between protease and TF constructs on neighboring membranes. We also attempted to generate a HiLITR TF for the peroxisomal membrane.…”

Section: Resultsmentioning

confidence: 99%

An engineered transcriptional reporter of protein localization identifies regulators of mitochondrial and ER membrane protein trafficking in high-throughput CRISPRi screens

Coukos

Yao

Sanchez

et al. 2021

eLife

View full text Add to dashboard Cite

The trafficking of specific protein cohorts to correct subcellular locations at correct times is essential for every signaling and regulatory process in biology. Gene perturbation screens could provide a powerful approach to probe the molecular mechanisms of protein trafficking, but only if protein localization or mislocalization can be tied to a simple and robust phenotype for cell selection, such as cell proliferation or fluorescence-activated cell sorting (FACS). To empower the study of protein trafficking processes with gene perturbation, we developed a genetically-encoded molecular tool named HiLITR. HiLITR converts protein colocalization into proteolytic release of a membrane-anchored transcription factor, which drives the expression of a chosen reporter gene. Using HiLITR in combination with FACS-based CRISPRi screening in human cell lines, we identified genes that influence the trafficking of mitochondrial and ER tail-anchored proteins. We show that loss of the SUMO E1 component SAE1 results in mislocalization and destabilization of many mitochondrial tail-anchored proteins. We also demonstrate a distinct regulatory role for EMC10 in the ER membrane complex, opposing the transmembrane-domain insertion activity of the complex. Through transcriptional integration of complex cellular functions, HiLITR expands the scope of biological processes that can be studied by genetic perturbation screening technologies.

show abstract

“…S4G). This may be a function of the prevalence of mitochondria-peroxisome contact sites (Chen et al, 2020), which could produce cross-talk between protease and TF constructs on neighboring membranes.…”

Section: Text S4a Hilitr At the Peroxisomal Membrane Related To Figures S4f/gmentioning

confidence: 99%

An engineered transcriptional reporter of protein localization identifies regulators of mitochondrial and ER membrane protein trafficking in high-throughput screens

Coukos

Yao

Sánchez

et al. 2021

Preprint

View full text Add to dashboard Cite

The trafficking of specific protein cohorts to the correct subcellular location at the correct time is essential for every signaling and regulatory process in biology. Gene perturbation screens could provide a powerful approach to probe the molecular mechanisms of protein trafficking, but only if protein localization or mislocalization can be tied to a simple and robust phenotype for cell selection, such as cell proliferation or FACS. To broadly empower the study of protein trafficking processes with gene perturbation, we developed a genetically-encoded molecular tool named HiLITR. HiLITR converts protein colocalization into proteolytic release of a membrane-anchored transcription factor, which drives the expression of a chosen reporter gene. Using HiLITR in combination with FACS-based CRISPRi screening in human cell lines, we identify genes that influence the trafficking of mitochondrial and ER tail-anchored proteins. We show that loss of the SUMO E1 component SAE1 results in the mislocalization and destabilization of mitochondrial tail-anchored proteins. We also demonstrate a distinct regulatory role for EMC10 in the ER membrane complex, opposing the transmembrane-domain insertion activity of the complex. Through transcriptional integration of complex cellular functions, HiLITR expands the scope of biological processes that can be studied by genetic perturbation screening technologies.

show abstract

Peroxisomal Membrane Contact Sites in Mammalian Cells

Cited by 22 publications

References 91 publications

Peroxisomal ABC Transporters: An Update

Peroxisomal ABC Transporters: An Update

An engineered transcriptional reporter of protein localization identifies regulators of mitochondrial and ER membrane protein trafficking in high-throughput CRISPRi screens

An engineered transcriptional reporter of protein localization identifies regulators of mitochondrial and ER membrane protein trafficking in high-throughput screens

Contact Info

Product

Resources

About