Author Correction: Efficient proximity labeling in living cells and organisms with TurboID

Branon, Tess C; Bosch, Justin A.; Sanchez, Ariana D.; Udeshi, Namrata D.; Svinkina, Tanya; Carr, Steven A.; Feldman, Jessica L.; Perrimon, Norbert; Ting, Alice Y.

doi:10.1038/s41587-019-0355-0

Cited by 11 publications

(7 citation statements)

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“…PPIs in the secretory pathway mediate the folding, modification, and transportation of secreted proteins (Bonifacino & Glick, 2004; Calakos et al, 1994; Ikawa et al, 1997; Pearl & Prodromou, 2006; Watanabe et al, 2019). Incidentally, co‐expression analysis has linked certain PTMs across the secretome to the expression of their responsible enzymes.…”

Section: Resultsmentioning

confidence: 99%

“…BioID2 requires less biotin supplementation and exhibits enhanced labeling of proximate protein , allowing for BioID to be introduced to new systems where biotinylation supplementation may not be easily accomplished (Sears et al, 2019). More recently, two promiscuous mutants of biotin ligase, TurboID and miniTurbo, have been developed to catalyze proximity labeling even with much greater efficiency (Branon et al, 2020) and therefore, can be considered as an effective method when proximal labeling of the endomembrane organelles is desired. It is also possible that the coverage of biotin labeling may be limited in the early processes in the secretory pathway due to the maturation process of the biotin ligase, that is, biotinylation only can occur once the biotin ligase has been fully functional.…”

Section: Discussionmentioning

confidence: 99%

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In situ detection of protein interactions for recombinant therapeutic enzymes

Samoudi

Kuo

Robinson

et al. 2020

Biotech & Bioengineering

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Despite their therapeutic potential, many protein drugs remain inaccessible to patients since they are difficult to secrete. Each recombinant protein has unique physicochemical properties and requires different machinery for proper folding, assembly, and posttranslational modifications (PTMs). Here we aimed to identify the machinery supporting recombinant protein secretion by measuring the protein–protein interaction (PPI) networks of four different recombinant proteins (SERPINA1, SERPINC1, SERPING1, and SeAP) with various PTMs and structural motifs using the proximity‐dependent biotin identification (BioID) method. We identified PPIs associated with specific features of the secreted proteins using a Bayesian statistical model and found proteins involved in protein folding, disulfide bond formation, and N‐glycosylation were positively correlated with the corresponding features of the four model proteins. Among others, oxidative folding enzymes showed the strongest association with disulfide bond formation, supporting their critical roles in proper folding and maintaining the ER stability. Knockdown of disulfide‐isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds. Proximity‐dependent labeling successfully identified the transient interactions supporting synthesis of secreted recombinant proteins and refined our understanding of key molecular mechanisms of the secretory pathway during recombinant protein production.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

In situ detection of protein interactions for recombinant therapeutic enzymes

Samoudi

Kuo

Robinson

et al. 2020

Biotech & Bioengineering

View full text Add to dashboard Cite

show abstract

“…BioID2 was shown to improve localization and was more sensitive to a lower biotin concentration, potentially allowing for BioID to be introduced to new systems where biotinylation supplementation may not be easily accomplished 52 . More recently, Ting's group has developed two promiscuous mutants of biotin ligase, TurboID and miniTurbo, which catalyze proximity labeling even with much greater efficiency 54 . Therefore, BioID2 or TurboID can be considered an effective method when proximal labeling of the endomembrane organelles is desired.…”

Section: Discussionmentioning

confidence: 99%

In situ detection of protein interactions for recombinant therapeutic enzymes

Samoudi

Kuo

Robinson

et al. 2020

Preprint

View full text Add to dashboard Cite

Despite their therapeutic potential, many protein drugs remain inaccessible to patients since they are difficult to secrete. Each recombinant protein has unique physicochemical properties and requires different machinery for proper folding, assembly, and post-translational modifications (PTMs). Here we aimed to identify the machinery supporting recombinant protein secretion by measuring the protein-protein interaction (PPI) networks of four different recombinant proteins (SERPINA1, SERPINC1, SERPING1 and SeAP) with various PTMs and structural motifs using the proximitydependent biotin identification (BioID) method. We identified PPIs associated with specific features of the secreted proteins using a Bayesian statistical model, and found proteins involved in protein folding, disulfide bond formation and N-glycosylation were positively correlated with the corresponding features of the four model proteins. Among others, oxidative folding enzymes showed the strongest association with disulfide bond formation, supporting their critical roles in proper folding and maintaining the ER stability. Knock down of ERP44, a measured interactor with the highest fold change, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds. Proximity-dependent labeling successfully identified the transient interactions supporting synthesis of secreted recombinant proteins and refined our understanding of key molecular mechanisms of the secretory pathway during recombinant protein production.

show abstract

“…Furthermore, transient interactions can be captured, and at the same time, additional information of subcellular localisation and proteins in the proximity of the targeted protein (e.g. part of the protein complex) will be detected [51][52][53]. Doubtless, it is an upgrade of the similar techniques applied before from which the whole field can benefit.…”

Section: Ros Assaysmentioning

confidence: 99%