TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion

Janine McCaughey; Vicky J Miller; Nicola Stevenson; Anna Brown; Annika Budnik; Kate Heesom; Dominic R Alibhai; David Stephens

doi:10.1016/j.celrep.2016.04.062

TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion

Janine McCaughey, Vicky J Miller, Nicola Stevenson, Anna Brown, Annika Budnik, Kate Heesom, Dominic R Alibhai, David Stephens

Research output: Contribution to journal › Article (Academic Journal) › peer-review

33 Citations (Scopus)

334 Downloads (Pure)

Abstract

Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.

Original language	English
Article number	15
Pages (from-to)	1648-59
Number of pages	12
Journal	Cell Reports
Volume	15
Issue number	8
Early online date	12 May 2016
DOIs	https://doi.org/10.1016/j.celrep.2016.04.062
Publication status	Published - 24 May 2016

Structured keywords

BrisSynBio
Bristol BioDesign Institute

Keywords

Synthetic biology

Access to Document

10.1016/j.celrep.2016.04.062

Full-text PDF (final published version)
This is the final published version of the article (version of record). It first appeared online via Elsevier (Cell) at http://www.cell.com/cell-reports/fulltext/S2211-1247%2816%2930506-X
Final published version, 4.93 MBLicence: CC BY
Analysis_of_STED_data_2015_10_29Other version, 12.3 KBLicence: CC BY
Movie for Fig 3BOther version, 3.56 MBLicence: CC BY
Movie for Fig 3AOther version, 1.36 MBLicence: CC BY

Embargoed Document

McCaughey et al 2016 Author version
Accepted author manuscript, 7.76 MB
Licence: CC BY
Request copy

4 Finished

Photo-oxidation and cryofluorescence for Correlative Light Electron Microscopy
Stephens, D. J.
1/12/13 → 1/12/16
Project: Research
The Golgi apparatus as an initiator of ciliogenesis
Stephens, D. J.
4/11/13 → 3/11/16
Project: Research
The role of Sec16A in driving secretory cargo export from the endoplasmic reticulum.
Stephens, D. J.
9/07/12 → 9/07/15
Project: Research

Proteomics Facility
Kate Heesom (Manager)
Faculty of Life Sciences
Facility/equipment: Facility
Wolfson Bioimaging Facility
Mark Jepson (Manager)
Faculty of Life Sciences
Facility/equipment: Facility

Professor David J Stephens
- David.Stephens@bristol.ac.uk
- Fundamental Bioscience
- School of Biochemistry - Professor of Cell Biology
- Dynamic Cell Biology
Person: Academic , Member

Cite this

@article{b8eece44af104bc183ee0288649cd2aa,

title = "TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion",

abstract = "Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.",

keywords = "Synthetic biology",

author = "Janine McCaughey and Miller, {Vicky J} and Nicola Stevenson and Anna Brown and Annika Budnik and Kate Heesom and Alibhai, {Dominic R} and David Stephens",

year = "2016",

month = may,

day = "24",

doi = "10.1016/j.celrep.2016.04.062",

language = "English",

volume = "15",

pages = "1648--59",

journal = "Cell Reports",

issn = "2211-1247",

publisher = "Cell Press",

number = "8",

}

TY - JOUR

T1 - TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion

AU - McCaughey, Janine

AU - Miller, Vicky J

AU - Stevenson, Nicola

AU - Brown, Anna

AU - Budnik, Annika

AU - Heesom, Kate

AU - Alibhai, Dominic R

AU - Stephens, David

PY - 2016/5/24

Y1 - 2016/5/24

N2 - Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.

AB - Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.

KW - Synthetic biology

U2 - 10.1016/j.celrep.2016.04.062

DO - 10.1016/j.celrep.2016.04.062

M3 - Article (Academic Journal)

C2 - 27184855

VL - 15

SP - 1648

EP - 1659

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 8

M1 - 15

ER -

TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion

Abstract

Structured keywords

Keywords

Access to Document

Embargoed Document

Fingerprint

Projects

Photo-oxidation and cryofluorescence for Correlative Light Electron Microscopy

The Golgi apparatus as an initiator of ciliogenesis

The role of Sec16A in driving secretory cargo export from the endoplasmic reticulum.

Equipment

Proteomics Facility

Wolfson Bioimaging Facility

Profiles

Professor David J Stephens

Cite this