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PreprintCited by 20Cellular transport and secretionNuclear Structure and FunctionMicrotubule and mitosis dynamics

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A Hollow TFG Condensate Spatially Compartmentalizes the Early Secretory Pathway

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Wegeng, William R., Bogus, Savannah M., Ruiz, Miguel, Chavez, Sindy R., Noori, Khalid S. M., Niesman, Ingrid R., Ernst, Andreas M.·2024·Nature Communications
DOI 10.1101/2024.03.26.586876PMC PMC12009431

Preprint — published as 10.1038/s41467-025-59118-1

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Abstract

Summary: In the early secretory pathway, endoplasmic reticulum (ER) and Golgi membranes form a nearly spherical interface. In this ribosome-excluding zone, bidirectional transport of cargo coincides with a spatial segregation of anterograde and retrograde carriers by an unknown mechanism. We show that at physiological conditions, Trk-fused gene (TFG) self-organizes to form a hollow, anisotropic condensate that matches the dimensions of the ER-Golgi interface. Regularly spaced hydrophobic residues in TFG control the condensation mechanism and result in a porous condensate surface. We find that TFG condensates act as a molecular sieve, enabling molecules corresponding to the size of anterograde coats (COPII) to access the condensate interior while restricting retrograde coats (COPI). We propose that a hollow TFG condensate structures the ER-Golgi interface to create a diffusion-limited space for bidirectional transport. We further propose that TFG condensates optimize membrane flux by insulating secretory carriers in their lumen from retrograde carriers outside TFG cages.

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Fig. 1 Recombinant TFG assembles into anisotropic, hollow condensates in vitro. a Representative 4-color micrograph of an individual ERES/cis-Golgi unit. HeLa cells were transfected with mGFP-Sec16L (green), FLAG-TFG-SNAP (cyan) (labeled with SNAP-Cell 647-SiR), and immunostained for endogenous GM130 (gray) and TANGO1 (red). Scale bar 1 µm. b Fluorescence intensity line scan of 4-color ERES/cis-Golgi unit (averaged and normalized to TANGO1, n = 4). Schematic of localizations detected in the representative unit (a) is given. c Representative purity of peak TFG elutions from concentration/salt exchange (Coomassie staining). d Confocal time series of increasing concentration of TFG-mEGFP-FLAG at the edge of an evaporating 10 µL sessile droplet, 150 mM KCl. Scale bar 5 μm. Starting concentration ~100 nM. e TFG-mEGFP-FLAG at 430 nM spontaneously assembles into ‘sponge-like’, anisotropic condensates (HEPES/KOH pH 7.3; 150 mM KCl; 20% (v/v) PEG 8 kDa; confocal microscopy). Scale bar 5 µm. Individual TFG condensate, Z-step 125 nm. Scale bar 500 nm. f Schematic depicting the ER–Golgi interface (targets for immunolabeling at ERES: red; cis-Golgi: grey. g ERES to cis-Golgi distance measured between immunolabeled GM130 and TANGO1, mean = 269, n = 120, vs diameter of individual hollow TFG condensates in vitro, mean = 341, n = 175. h Determination of the saturation concentration required for the formation of hollow TFG condensates (in the absence of crowding agents). Representative micrographs depicting the distribution of TFG below and above the saturation concentration of 100 nM. Higher concentrations of TFG yield inverted phases (right micrograph). Dilute phase (left) shown at <5 nM, dense phase (middle) shown at 200 nM, inverted phase (right) shown at 6.4 µM. Red diamonds indicate saturation concentration and average cellular concentration of TFG. Scale bars 5 µm. Source data are provided as a Source Data file.
Fig. 1 Recombinant TFG assembles into anisotropic, hollow condensates in vitro. a Representative 4-color micrograph of an individual ERES/cis-Golgi unit. HeLa cells were transfected with mGFP-Sec16L (green), FLAG-TFG-SNAP (cyan) (labeled with SNAP-Cell 647-SiR), and immunostained for endogenous GM130 (gray) and TANGO1 (red). Scale bar 1 µm. b Fluorescence intensity line scan of 4-color ERES/cis-Golgi unit (averaged and normalized to TANGO1, n = 4). Schematic of localizations detected in the representative unit (a) is given. c Representative purity of peak TFG elutions from concentration/salt exchange (Coomassie staining). d Confocal time series of increasing concentration of TFG-mEGFP-FLAG at the edge of an evaporating 10 µL sessile droplet, 150 mM KCl. Scale bar 5 μm. Starting concentration ~100 nM. e TFG-mEGFP-FLAG at 430 nM spontaneously assembles into ‘sponge-like’, anisotropic condensates (HEPES/KOH pH 7.3; 150 mM KCl; 20% (v/v) PEG 8 kDa; confocal microscopy). Scale bar 5 µm. Individual TFG condensate, Z-step 125 nm. Scale bar 500 nm. f Schematic depicting the ER–Golgi interface (targets for immunolabeling at ERES: red; cis-Golgi: grey. g ERES to cis-Golgi distance measured between immunolabeled GM130 and TANGO1, mean = 269, n = 120, vs diameter of individual hollow TFG condensates in vitro, mean = 341, n = 175. h Determination of the saturation concentration required for the formation of hollow TFG condensates (in the absence of crowding agents). Representative micrographs depicting the distribution of TFG below and above the saturation concentration of 100 nM. Higher concentrations of TFG yield inverted phases (right micrograph). Dilute phase (left) shown at <5 nM, dense phase (middle) shown at 200 nM, inverted phase (right) shown at 6.4 µM. Red diamonds indicate saturation concentration and average cellular concentration of TFG. Scale bars 5 µm. Source data are provided as a Source Data file.CC BY · PubMed Central
Fig. 2 Endogenous tagging and overexpression confirm assembly of TFG into anisotropic condensates that disassemble during mitosis. a Representative widefield micrograph of HeLa cells with homozygous endogenously tagged TFG::mClover-FLAG. Scale bar 10 μm. Magnified micrograph (dashed box in cell overview): individual TFG condensate. Scale bar 500 nm. b Quantification of the diameter of endogenous TFG condensates = 30. The dashed line represents the average of in vitro condensate diameter (341 nm ± 87) and the dotted line represents the average of endogenous ER/Golgi interface diameter (269 nm), for reference. c Qualitative fluorescence recovery after photobleaching (FRAP) of a TFG condensate. Scale bar 500 nm. d Left: live-cell confocal microscopy of large individual condensates within HeLa cells transfected with TFG-mEGFP-FLAG. Scale bar 5 μm. Middle: STED micrograph of large individual condensates within HeLa cells transfected with TFG-mEGFP-FLAG. Scale bar 2 μm. Right: 3D-structured illumination microscopy (3D-SIM) of large individual condensates within HeLa cells transfected with TFG-tGFP. Scale bar 500 nm. e Representative micrographs of partial and full FRAP experiments on overexpressed TFG condensates in HeLa cells. f Quantification of average condensate recovery rates for partial (n = 33) and full (n = 30) FRAP; normalized to pre-bleach (=100) and post-bleach intensity (=0). Error bars represent standard deviation. g Representative live-cell imaging of TFG condensate fusion dynamics. h Line scan of condensate depicted in (g). Source data are provided as a Source Data file.
Fig. 2 Endogenous tagging and overexpression confirm assembly of TFG into anisotropic condensates that disassemble during mitosis. a Representative widefield micrograph of HeLa cells with homozygous endogenously tagged TFG::mClover-FLAG. Scale bar 10 μm. Magnified micrograph (dashed box in cell overview): individual TFG condensate. Scale bar 500 nm. b Quantification of the diameter of endogenous TFG condensates = 30. The dashed line represents the average of in vitro condensate diameter (341 nm ± 87) and the dotted line represents the average of endogenous ER/Golgi interface diameter (269 nm), for reference. c Qualitative fluorescence recovery after photobleaching (FRAP) of a TFG condensate. Scale bar 500 nm. d Left: live-cell confocal microscopy of large individual condensates within HeLa cells transfected with TFG-mEGFP-FLAG. Scale bar 5 μm. Middle: STED micrograph of large individual condensates within HeLa cells transfected with TFG-mEGFP-FLAG. Scale bar 2 μm. Right: 3D-structured illumination microscopy (3D-SIM) of large individual condensates within HeLa cells transfected with TFG-tGFP. Scale bar 500 nm. e Representative micrographs of partial and full FRAP experiments on overexpressed TFG condensates in HeLa cells. f Quantification of average condensate recovery rates for partial (n = 33) and full (n = 30) FRAP; normalized to pre-bleach (=100) and post-bleach intensity (=0). Error bars represent standard deviation. g Representative live-cell imaging of TFG condensate fusion dynamics. h Line scan of condensate depicted in (g). Source data are provided as a Source Data file.CC BY · PubMed Central
Fig. 3 TFG is regulated by phosphorylation across the cell cycle. a Representative micrograph of interphase (left) and mitotic (right) HeLa cells with endogenously tagged TFG. Cells were stained with Hoechst (magenta). Scale bar 10 μm. b Micrographs of recombinant TFG-162-240-mEGFP-FLAG purified from synchronized interphase or mitotic Expi293F cells. Mitosis-derived protein was treated with lambda protein phosphatase (λPP) where indicated. Scale bar 10 μm; inset 500 nm c Schematic depicting predicted phosphorylation sites within TFG (bottom): serine/threonine, orange; tyrosine, cyan, and depicting confidently identified phosphorylation sites found via mass spectrometry in TFG (top) with mitotic phosphorylation site depicted with red/bolded ‘P’. Putative phosphorylation sites were predicted by NetPhos-3.0. d Representative anti-TFG Western blot of PhosTag gel depicting purified recombinant TFG-mEGFP-FLAG derived from synchronized cells in interphase (I) or mitosis (M) as indicated. Arrows indicate species that are less abundant (lowest arrow) or more abundant (upper arrows). Blank lane between each condition was cropped. e Representative micrograph of phosphomimetic TFG-mEGFP-FLAG 24 h post-transfection in HeLa cells. Widefield microscopy, Z-slice, scale bar 10 µm. f Representative widefield deconvolution micrographs of interphase (upper) and mitotic (lower) HeLa cells overexpressing TFG-mEGFP-FLAG (left), TFG-T87A-mEGFP-FLAG (phosphor-dead) (middle), or TFG-T87E-mEGFP-FLAG (phosphomimetic) (right). Cells were stained with Hoechst (magenta). Scale bar 10 µm. 90% of mitotic cells expressing wild-type TFG (n = 24) or TFG-T87E (n = 10) were able to fully dissolve foci, in contrast to 65% in T87A-expressing cells (n = 26). At least three independent experiments were performed to obtain the replicates for each condition. Source data are provided as a Source Data file.
Fig. 3 TFG is regulated by phosphorylation across the cell cycle. a Representative micrograph of interphase (left) and mitotic (right) HeLa cells with endogenously tagged TFG. Cells were stained with Hoechst (magenta). Scale bar 10 μm. b Micrographs of recombinant TFG-162-240-mEGFP-FLAG purified from synchronized interphase or mitotic Expi293F cells. Mitosis-derived protein was treated with lambda protein phosphatase (λPP) where indicated. Scale bar 10 μm; inset 500 nm c Schematic depicting predicted phosphorylation sites within TFG (bottom): serine/threonine, orange; tyrosine, cyan, and depicting confidently identified phosphorylation sites found via mass spectrometry in TFG (top) with mitotic phosphorylation site depicted with red/bolded ‘P’. Putative phosphorylation sites were predicted by NetPhos-3.0. d Representative anti-TFG Western blot of PhosTag gel depicting purified recombinant TFG-mEGFP-FLAG derived from synchronized cells in interphase (I) or mitosis (M) as indicated. Arrows indicate species that are less abundant (lowest arrow) or more abundant (upper arrows). Blank lane between each condition was cropped. e Representative micrograph of phosphomimetic TFG-mEGFP-FLAG 24 h post-transfection in HeLa cells. Widefield microscopy, Z-slice, scale bar 10 µm. f Representative widefield deconvolution micrographs of interphase (upper) and mitotic (lower) HeLa cells overexpressing TFG-mEGFP-FLAG (left), TFG-T87A-mEGFP-FLAG (phosphor-dead) (middle), or TFG-T87E-mEGFP-FLAG (phosphomimetic) (right). Cells were stained with Hoechst (magenta). Scale bar 10 µm. 90% of mitotic cells expressing wild-type TFG (n = 24) or TFG-T87E (n = 10) were able to fully dissolve foci, in contrast to 65% in T87A-expressing cells (n = 26). At least three independent experiments were performed to obtain the replicates for each condition. Source data are provided as a Source Data file.CC BY · PubMed Central
Fig. 4 Hydrophobic ‘sticker’ residues control the anisotropic condensation mechanism of TFG. a Schematic depicting domains present within TFG: PB1 domain, blue; alpha helices, green; Gln-rich region, purple; intrinsically disordered region (IDR), gray. Individual IDRs are defined as: IDR1 (net acidic), IDR2 (Gln-rich), IDR3 (net basic). Residues for truncated constructs are depicted to scale. b All truncated constructs except for residues 1-123 of TFG support the formation of lumen-containing (anisotropic) condensates. Representative micrographs are given. Overview scale bars 5 µm; insets 500 nm. c Quantification of the average peak-to-peak diameter of condensates formed by individual truncations of TFG. TFG; TFG 124–240: n = 124; TFG 124–161: n = 79; TFG 162–240: n = 176; TFG 241–359: n = 93; TFG 360–400: n = 107. The dashed line represents the average TFG 1–400 condensate diameter for reference. Two-tailed unpaired t-tests (TFG-124–240: p < 0.0001, TFG-185–240: p = 0.0006, TFG-241–359: p = 0.0011, TFG-360–400: p < 0.0001). d TFG phase diagram probing increasing concentrations of KCl vs PEG 8 kDa as a crowding agent. TFG-mEGFP-FLAG: 70 nM; HEPES/KOH pH 7.3; X mM KCl as indicated; X% (v/v) PEG 8 kDa as indicated. Scale bar 10 µm. e Schematic based on an AlphaFold prediction of TFG structure color-coded for hydrophobicity (red: max; blue: min). Domain annotations and the position of hydrophobic residues (‘stickers’) within IDRs are given. f Widefield deconvolution micrographs of HeLa cells transfected with TFG-mEGFP-FLAG and TFG-1–400-w/o ‘stickers’-mEGFP-FLAG, respectively. Scale bar 10 µm. g Representative micrographs of HeLa cells transfected with TFG-mEGFP-FLAG shifted to the indicated temperatures (top) and time-lapse of a single cell shifted through indicated temperatures (bottom). Scale bar 10 µm. h Quantification of condensate circularity at specific temperatures. Two-tailed unpaired t-tests (*p = 0.0378, ***p = 0.0003, ****p < 0.0001) i Micrographs of TFG-162-240-mEGFP-FLAG in vitro incubated at indicated temperatures. Representative of three experiments. Scale bar 5 µm. Source data are provided as a Source Data file.
Fig. 4 Hydrophobic ‘sticker’ residues control the anisotropic condensation mechanism of TFG. a Schematic depicting domains present within TFG: PB1 domain, blue; alpha helices, green; Gln-rich region, purple; intrinsically disordered region (IDR), gray. Individual IDRs are defined as: IDR1 (net acidic), IDR2 (Gln-rich), IDR3 (net basic). Residues for truncated constructs are depicted to scale. b All truncated constructs except for residues 1-123 of TFG support the formation of lumen-containing (anisotropic) condensates. Representative micrographs are given. Overview scale bars 5 µm; insets 500 nm. c Quantification of the average peak-to-peak diameter of condensates formed by individual truncations of TFG. TFG; TFG 124–240: n = 124; TFG 124–161: n = 79; TFG 162–240: n = 176; TFG 241–359: n = 93; TFG 360–400: n = 107. The dashed line represents the average TFG 1–400 condensate diameter for reference. Two-tailed unpaired t-tests (TFG-124–240: p < 0.0001, TFG-185–240: p = 0.0006, TFG-241–359: p = 0.0011, TFG-360–400: p < 0.0001). d TFG phase diagram probing increasing concentrations of KCl vs PEG 8 kDa as a crowding agent. TFG-mEGFP-FLAG: 70 nM; HEPES/KOH pH 7.3; X mM KCl as indicated; X% (v/v) PEG 8 kDa as indicated. Scale bar 10 µm. e Schematic based on an AlphaFold prediction of TFG structure color-coded for hydrophobicity (red: max; blue: min). Domain annotations and the position of hydrophobic residues (‘stickers’) within IDRs are given. f Widefield deconvolution micrographs of HeLa cells transfected with TFG-mEGFP-FLAG and TFG-1–400-w/o ‘stickers’-mEGFP-FLAG, respectively. Scale bar 10 µm. g Representative micrographs of HeLa cells transfected with TFG-mEGFP-FLAG shifted to the indicated temperatures (top) and time-lapse of a single cell shifted through indicated temperatures (bottom). Scale bar 10 µm. h Quantification of condensate circularity at specific temperatures. Two-tailed unpaired t-tests (*p = 0.0378, ***p = 0.0003, ****p < 0.0001) i Micrographs of TFG-162-240-mEGFP-FLAG in vitro incubated at indicated temperatures. Representative of three experiments. Scale bar 5 µm. Source data are provided as a Source Data file.CC BY · PubMed Central
Fig. 5 Hollow TFG condensates are porous and select for macromolecules of defined sizes. a Left: SEM of TFG-162–240-mEGFP-FLAG condensates. Scale bar 500 nm. Middle: transmission electron micrograph (TEM) of a single TFG-162–240-mEGFP-FLAG condensate (no crowding agents or negative staining; LUT inverted). Scale bar 100 nm. Right: Magnification of the porous surface of TFG condensates (boxed area in middle panel, inverted LUT). Scale bar 25 nm. b Quantification of average pore size of TFG condensates micrograph (n = 79). c Permeability of TFG-185–240-mEGFP-FLAG and TFG-185–240-w/o ‘stickers’ -mEGFP-FLAG condensates (induced with 20 % (v/v) PEG 8 kDa) for fluorescent dextran-TMR species of various sizes. Representative confocal micrographs are given for 155 kDa and 500 kDa dextran. Normalized line intensities for representative merged images are given with TFG in green and dextran species in red. Scale bar 5 µm, zoom in 1 µm. Representative of at least three experiments. d Graph depicts the molecular weight range of dextrans that can access the lumen of TFG condensates (included: detected in the lumen of TFG condensates, white-filled circles; excluded: sequestered from TFG condensates, back circles). Source data are provided as a Source Data file.
Fig. 5 Hollow TFG condensates are porous and select for macromolecules of defined sizes. a Left: SEM of TFG-162–240-mEGFP-FLAG condensates. Scale bar 500 nm. Middle: transmission electron micrograph (TEM) of a single TFG-162–240-mEGFP-FLAG condensate (no crowding agents or negative staining; LUT inverted). Scale bar 100 nm. Right: Magnification of the porous surface of TFG condensates (boxed area in middle panel, inverted LUT). Scale bar 25 nm. b Quantification of average pore size of TFG condensates micrograph (n = 79). c Permeability of TFG-185–240-mEGFP-FLAG and TFG-185–240-w/o ‘stickers’ -mEGFP-FLAG condensates (induced with 20 % (v/v) PEG 8 kDa) for fluorescent dextran-TMR species of various sizes. Representative confocal micrographs are given for 155 kDa and 500 kDa dextran. Normalized line intensities for representative merged images are given with TFG in green and dextran species in red. Scale bar 5 µm, zoom in 1 µm. Representative of at least three experiments. d Graph depicts the molecular weight range of dextrans that can access the lumen of TFG condensates (included: detected in the lumen of TFG condensates, white-filled circles; excluded: sequestered from TFG condensates, back circles). Source data are provided as a Source Data file.CC BY · PubMed Central
Fig. 6 TFG condensates insulate COPII from COPI coats. a Representative micrograph of HeLa cells transfected with FLAG-TFG-SNAP: Snap-Cell 647 SiR, mEmerald-Sec23A (top), EYFP-Sec24C (bottom), and immunostained for β-COP, a component of coatomer. Scale bar 1 µm. The experimental setup was reproduced seven times. b Permeability of TFG-162–240-mEGFP-FLAG condensates (induced with 10% (v/v) PEG 8 kDa) for E. coli ribosomes labeled with NHS-SiR. Line scans depict normalized line intensity with TFG in green and ribosomes in red. Scale bar 1 µm. Representative of at least three separate experiments. c Electron micrographs of (left) control siRNA and nocodazole and (middle/right) TFG knockdown and nocodazole. Nucleus (N), yellow; Golgi-associated mitochondria, green; Golgi-associated ER, cyan; putative Golgi stacks/tubules, purple; Golgi-associated vesicles, red. d Quantification of vesicles per µm2 of multiple selected Golgi stack areas from micrographs depicted in c. p = 0.0025. See “Methods”. e Model depicting the role of TFG at the ER–Golgi interface: TFG self-organizes into 300-nm condensates that are hollow. Their porous surface allows for COPII coat components (Sec23/24, Sec13/31, both complexes < 250 kDa) to access the lumen of TFG condensates, forming anterograde carriers. The retrograde carrier-forming COPI coat (550 kDa total) cannot access the lumen of TFG condensates. This may lead to a spatial segregation of anterograde from retrograde traffic, and the creation of a diffusion-limited space for bidirectional transport at the ER–Golgi interface. Source data are provided as a Source Data file.
Fig. 6 TFG condensates insulate COPII from COPI coats. a Representative micrograph of HeLa cells transfected with FLAG-TFG-SNAP: Snap-Cell 647 SiR, mEmerald-Sec23A (top), EYFP-Sec24C (bottom), and immunostained for β-COP, a component of coatomer. Scale bar 1 µm. The experimental setup was reproduced seven times. b Permeability of TFG-162–240-mEGFP-FLAG condensates (induced with 10% (v/v) PEG 8 kDa) for E. coli ribosomes labeled with NHS-SiR. Line scans depict normalized line intensity with TFG in green and ribosomes in red. Scale bar 1 µm. Representative of at least three separate experiments. c Electron micrographs of (left) control siRNA and nocodazole and (middle/right) TFG knockdown and nocodazole. Nucleus (N), yellow; Golgi-associated mitochondria, green; Golgi-associated ER, cyan; putative Golgi stacks/tubules, purple; Golgi-associated vesicles, red. d Quantification of vesicles per µm2 of multiple selected Golgi stack areas from micrographs depicted in c. p = 0.0025. See “Methods”. e Model depicting the role of TFG at the ER–Golgi interface: TFG self-organizes into 300-nm condensates that are hollow. Their porous surface allows for COPII coat components (Sec23/24, Sec13/31, both complexes < 250 kDa) to access the lumen of TFG condensates, forming anterograde carriers. The retrograde carrier-forming COPI coat (550 kDa total) cannot access the lumen of TFG condensates. This may lead to a spatial segregation of anterograde from retrograde traffic, and the creation of a diffusion-limited space for bidirectional transport at the ER–Golgi interface. Source data are provided as a Source Data file.CC BY · PubMed Central

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Metadata

Authors
Wegeng, W. R., Bogus, S. M., Ruiz, M., Chavez, S. R., Noori, K. S. M., Niesman, I. R., & Ernst, A. M.
Affiliations
  • University of California San Diego (US)
  • San Diego State University (US)
Corresponding author
Ernst, Andreas M.
ORCID
Venue
Nature Communications
Publisher
openRxiv
Published
2024-03-27
Volume
16
Issue
1
Pages
3715-3715
ISSN
2041-1723 (ISSN-L)
DOI
10.1101/2024.03.26.586876
PMC
PMC12009431
OpenAlex
W4409591571
Cited by
20
References
1
Citations by year
2026: 11 · 2025: 8 · 2024: 1
FWCI
9.44
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion, cc-by)
  • PubMed Central (submittedVersion, cc-by-nc)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • U.S. Department of Health and Human Services (R35GM142433)
  • National Institutes of Health (1s10od021724-01, 1s10od016234-01)
  • Directorate for Biological Sciences
  • University of California, San Diego (P30 NS047101)
  • National Institute of General Medical Sciences (GM133351, S10 OD016234, T32GM133351, R35GM142433)
  • National Institute of Neurological Disorders and Stroke (P30NS047101)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
TFG, liquid-liquid phase separation, biomolecular condensates, ER-Golgi interface, early secretory pathway, retrograde transport, anterograde transport, molecular sieves, hydrophobic residues, cell cycle regulation, permeate flux

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Wegeng, W. R., Bogus, S. M., Ruiz, M., Chavez, S. R., Noori, K. S. M., Niesman, I. R., & Ernst, A. M. (2024). A Hollow TFG Condensate Spatially Compartmentalizes the Early Secretory Pathway. Nature Communications. https://doi.org/10.1101/2024.03.26.586876