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Article ; Online: The C-terminus of the cargo receptor Erv14 affects COPII vesicle formation and cargo delivery.

Lagunas-Gomez, Daniel / Yañez-Dominguez, Carolina / Zavala-Padilla, Guadalupe / Barlowe, Charles / Pantoja, Omar

2023 Volume 136, Issue 3

Abstract: ... site (S134) at the C-terminus of Erv14. Mimicking phosphorylation of S134 (S134D) prevents ...

Abstract	The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little is known about how post-translational modification events regulate packaging of cargo into COPII vesicles. The Saccharomyces cerevisiae protein Erv14, also known as cornichon, belongs to a conserved family of cargo receptors required for the selection and ER export of transmembrane proteins. In this work, we show the importance of a phosphorylation consensus site (S134) at the C-terminus of Erv14. Mimicking phosphorylation of S134 (S134D) prevents the incorporation of Erv14 into COPII vesicles, delays cell growth, exacerbates growth of sec mutants, modifies ER structure and affects localization of several plasma membrane transporters. In contrast, the dephosphorylated mimic (S134A) had less deleterious effects, but still modifies ER structure and slows cell growth. Our results suggest that a possible cycle of phosphorylation and dephosphorylation is important for the correct functioning of Erv14.
MeSH term(s)	Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Membrane Proteins/metabolism ; Carrier Proteins/metabolism ; Membrane Transport Proteins/metabolism ; Biological Transport ; COP-Coated Vesicles/metabolism ; Protein Transport
Chemical Substances	Saccharomyces cerevisiae Proteins ; Membrane Proteins ; Carrier Proteins ; Membrane Transport Proteins
Language	English
Publishing date	2023-02-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260527
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Zs.MG 14: Show issues

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Article ; Online: Twenty-five years after coat protein complex II.

Barlowe, Charles

Molecular biology of the cell

2019 Volume 31, Issue 1, Page(s) 3–6

Abstract: In 1994, a convergence of ideas and collaborative research orchestrated by Randy Schekman led to the discovery of the coat protein complex II (COPII). In this Perspective, the chain of events enabling discovery of a new vesicle coat and progress on ... ...

Abstract	In 1994, a convergence of ideas and collaborative research orchestrated by Randy Schekman led to the discovery of the coat protein complex II (COPII). In this Perspective, the chain of events enabling discovery of a new vesicle coat and progress on understanding COPII budding mechanisms are considered.
MeSH term(s)	COP-Coated Vesicles/metabolism ; COP-Coated Vesicles/physiology ; Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Humans ; Protein Transport ; Vesicular Transport Proteins/metabolism
Chemical Substances	Vesicular Transport Proteins
Language	English
Publishing date	2019-12-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E19-11-0621
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 410: Show issues

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Article ; Online: Membrane trafficking: ER export encounters dualism.

Barlowe, Charles

Current biology : CB

2015 Volume 25, Issue 4, Page(s) R151–3

Abstract: Cytoplasmic coat protein complexes perform central roles in sorting protein constituents within the endomembrane system. A new study reveals that the COPII coat operates through dual recognition of signals in a sorting receptor and its bound cargo to ... ...

Abstract	Cytoplasmic coat protein complexes perform central roles in sorting protein constituents within the endomembrane system. A new study reveals that the COPII coat operates through dual recognition of signals in a sorting receptor and its bound cargo to promote efficient export from the endoplasmic reticulum.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Membrane Proteins/metabolism ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Membrane Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2015-02-16
Publishing country	England
Document type	Comment ; Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2015.01.017
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Article ; Online: Conserved juxtamembrane domains in the yeast golgin Coy1 drive assembly of a megadalton-sized complex and mediate binding to tethering and SNARE proteins.

Anderson, Nadine S / Barlowe, Charles

The Journal of biological chemistry

2019 Volume 294, Issue 25, Page(s) 9690–9705

Abstract: ... called golgins. Golgins are thought to form extended homodimers that are C-terminally anchored to Golgi ...

Abstract	The architecture and organization of the Golgi complex depend on a family of coiled-coil proteins called golgins. Golgins are thought to form extended homodimers that are C-terminally anchored to Golgi membranes, whereas their N termini extend into the cytoplasm to initiate vesicle capture. Previously, we reported that the
MeSH term(s)	Biological Transport ; Cell Membrane/metabolism ; Golgi Apparatus ; Golgi Matrix Proteins/genetics ; Golgi Matrix Proteins/metabolism ; Macromolecular Substances/metabolism ; Protein Binding ; SNARE Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Coy1 protein, S cerevisiae ; Golgi Matrix Proteins ; Macromolecular Substances ; SNARE Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2019-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.008107
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Article ; Online: Molecular dissection of the Erv41-Erv46 retrograde receptor reveals a conserved cysteine-rich region in Erv46 required for retrieval activity.

Keiser, Kristofer J / Barlowe, Charles

Molecular biology of the cell

2019 Volume 31, Issue 3, Page(s) 209–220

Abstract: The Erv41-Erv46 complex is a conserved retrograde cargo receptor that retrieves ER resident proteins from Golgi compartments in a pH-dependent manner. Here we functionally dissect the Erv46 subunit and define an approximately 60 residue cysteine-rich ... ...

Abstract	The Erv41-Erv46 complex is a conserved retrograde cargo receptor that retrieves ER resident proteins from Golgi compartments in a pH-dependent manner. Here we functionally dissect the Erv46 subunit and define an approximately 60 residue cysteine-rich region that is unique to the Erv46 family of proteins. This cysteine-rich region contains two vicinal cysteine pairs in CXXC and CCXXC configurations that are each required for retrieval activity in cells. Mutation of the individual cysteine residues produced stable Erv46 proteins that were partially reduced and form mixed-disulfide species on nonreducing gels. Conserved hydrophobic amino acids within the cysteine-rich region of Erv46 were also required for retrieval function in cells. In vitro binding experiments showed that this hydrophobic patch is required for direct cargo binding. Surprisingly, the Erv46 cysteine mutants continued to bind cargo in cell-free assays and produced an increased level of Erv46-cargo complexes in cell extracts suggesting that disulfide linkages in the cysteine-rich region perform a role in releasing bound cargo. On the basis of these findings, we propose that both pH and redox environments regulate cargo binding to a hydrophobic site within the cysteine-rich region of Erv46.
MeSH term(s)	Amino Acid Sequence ; Carrier Proteins/metabolism ; Conserved Sequence ; Cysteine/metabolism ; Disulfides/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation ; Protein Domains ; Protein Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Carrier Proteins ; Disulfides ; Erv41 protein, S cerevisiae ; Erv46 protein, S cerevisiae ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; Cysteine (K848JZ4886)
Language	English
Publishing date	2019-12-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E19-08-0484
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Association between time from esophageal food impaction to endoscopy and adverse events.

Redd, Walker D / McCallen, Justin D / Xue, Zeyun / Kiran, Akshatha / Barlowe, Trevor S / Reed, Craig C / Eluri, Swathi / Dellon, Evan S

Gastrointestinal endoscopy

2023 Volume 99, Issue 4, Page(s) 525–536.e3

Abstract: Background and aims: Guidelines recommend emergent or urgent EGD for esophageal food impaction (EFI), but data on how time to EGD impacts the risk of adverse events remain limited. We determined whether EFI-to-EGD time was associated with adverse events. ...

Abstract	Background and aims: Guidelines recommend emergent or urgent EGD for esophageal food impaction (EFI), but data on how time to EGD impacts the risk of adverse events remain limited. We determined whether EFI-to-EGD time was associated with adverse events. Methods: In this retrospective cohort study of patients with endoscopically confirmed EFI, adverse events were classified as esophageal (mucosal tear, bleeding, perforation) or extraesophageal (aspiration, respiratory compromise, hypotension, arrhythmia). Esophageal perforation and extraesophageal adverse events requiring intensive care unit admission were classified as serious adverse events. Baseline characteristics, event details, and procedural details were compared between patients with and without adverse events. Multivariable logistic regression was performed to assess for an association between EFI-to-EGD time and adverse events. Results: Of 188 patients with EFI, 22 (12%) had any adverse event and 2 (1%) had a serious adverse event. Patients with adverse events were older and more likely to have an esophageal motility disorder, to tolerate secretions at presentation, and to have a higher American Society of Anesthesiologists score. EFI-to-EGD time was similar in those with and without adverse events. On multivariable analysis, EFI-to-EGD time was not associated with adverse events (odds ratio, 1.00 [95% confidence interval, .97-1.04] for 1-hour increments; odds ratio, 1.03 [95% confidence interval, .86-1.24] for 6-hour increments). Results were similar after stratifying by eosinophilic esophagitis status and after adjusting for possible confounders. Conclusions: Because the time from EFI to EGD is not associated with adverse events, emergent EGD for EFI may be unnecessary, and other considerations may determine EGD timing.
MeSH term(s)	Humans ; Deglutition Disorders/etiology ; Retrospective Studies ; Eosinophilic Esophagitis/complications ; Endoscopy, Gastrointestinal/adverse effects
Language	English
Publishing date	2023-11-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	391583-9
ISSN	1097-6779 ; 0016-5107
ISSN (online)	1097-6779
ISSN	0016-5107
DOI	10.1016/j.gie.2023.11.005
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Zs.B 283: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 519: Show issues

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Article ; Online: ER sheets get roughed up.

Barlowe, Charles

Cell

2010 Volume 143, Issue 5, Page(s) 665–666

Abstract: The molecular machinery that shapes the endoplasmic reticulum's (ER's) membrane into ordered networks of "smooth" tubules and "rough" sheets is poorly defined. Shibata et al. (2010) now report that sheet-inducing proteins, such as Climp-63, are enriched ... ...

Abstract	The molecular machinery that shapes the endoplasmic reticulum's (ER's) membrane into ordered networks of "smooth" tubules and "rough" sheets is poorly defined. Shibata et al. (2010) now report that sheet-inducing proteins, such as Climp-63, are enriched in the "rough" ER by their association with membrane-bound ribosomes, whereas curvature-inducing proteins localize at highly bent edges of membrane sheets.
Language	English
Publishing date	2010-11-24
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2010.11.011
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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 58: Show issues

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Article ; Online: Atlasin GTPases shape up ER networks.

Barlowe, Charles

Developmental cell

2009 Volume 17, Issue 2, Page(s) 157–158

Abstract: The endoplasmic reticulum (ER) adopts a remarkable array of flattened membrane structures and branched tubular networks to support cellular function. Recent studies reveal that the integral membrane atlastin GTPases, which are linked to neurodegenerative ...

Abstract	The endoplasmic reticulum (ER) adopts a remarkable array of flattened membrane structures and branched tubular networks to support cellular function. Recent studies reveal that the integral membrane atlastin GTPases, which are linked to neurodegenerative diseases, catalyze membrane fusion and are required for the formation of branched membrane networks characteristic of the ER.
MeSH term(s)	Animals ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; GTP Phosphohydrolases/metabolism ; Humans ; Membrane Fusion/physiology
Chemical Substances	DNA-Binding Proteins ; Dp1 protein, Drosophila ; Drosophila Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; atl protein, Drosophila (EC 3.6.1.-)
Language	English
Publishing date	2009-07-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2009.07.019
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Zs.A 5742: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Overexpression of Sly41 suppresses COPII vesicle-tethering deficiencies by elevating intracellular calcium levels.

Mukherjee, Indrani / Barlowe, Charles

Molecular biology of the cell

2016 Volume 27, Issue 10, Page(s) 1635–1649

Abstract: SLY41 was identified as a multicopy suppressor of loss of Ypt1, a Rab GTPase essential for COPII vesicle tethering at the Golgi complex. SLY41 encodes a polytopic membrane protein with homology to a class of solute transporter proteins, but how ... ...

Abstract	SLY41 was identified as a multicopy suppressor of loss of Ypt1, a Rab GTPase essential for COPII vesicle tethering at the Golgi complex. SLY41 encodes a polytopic membrane protein with homology to a class of solute transporter proteins, but how overexpression suppresses vesicle-tethering deficiencies is not known. Here we show that Sly41 is efficiently packaged into COPII vesicles and actively cycles between the ER and Golgi compartments. SLY41 displays synthetic negative genetic interactions with PMR1, which encodes the major Golgi-localized Ca(2+)/Mn(2+) transporter and suggests that Sly41 influences cellular Ca(2+) and Mn(2+) homeostasis. Experiments using the calcium probe aequorin to measure intracellular Ca(2+) concentrations in live cells reveal that Sly41 overexpression significantly increases cytosolic calcium levels. Although specific substrates of the Sly41 transporter were not identified, our findings indicate that localized overexpression of Sly41 to the early secretory pathway elevates cytosolic calcium levels to suppress vesicle-tethering mutants. In vitro SNARE cross-linking assays were used to directly monitor the influence of Ca(2+) on tethering and fusion of COPII vesicles with Golgi membranes. Strikingly, calcium at suppressive concentrations stimulated SNARE-dependent membrane fusion when vesicle-tethering activity was reduced. These results show that calcium positively regulates the SNARE-dependent fusion stage of ER-Golgi transport.
MeSH term(s)	Amino Acid Sequence ; Biological Transport ; COP-Coated Vesicles/metabolism ; Calcium/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; GTP Phosphohydrolases/metabolism ; Golgi Apparatus/metabolism ; Intracellular Calcium-Sensing Proteins/metabolism ; Membrane Fusion ; Protein Binding ; SNARE Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism
Chemical Substances	Carrier Proteins ; Intracellular Calcium-Sensing Proteins ; SNARE Proteins ; Saccharomyces cerevisiae Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E15-10-0704
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 410: Show issues

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Article ; Online: Cargo Capture and Bulk Flow in the Early Secretory Pathway.

Barlowe, Charles / Helenius, Ari

Annual review of cell and developmental biology

2016 Volume 32, Page(s) 197–222

Abstract: Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and ...

Abstract	Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.
Language	English
Publishing date	2016-10-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1293750-2
ISSN	1530-8995 ; 1081-0706
ISSN (online)	1530-8995
ISSN	1081-0706
DOI	10.1146/annurev-cellbio-111315-125016
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