Cited by 309Cellular transport and secretionHemophilia Treatment and ResearchPlatelet Disorders and Treatments

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Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex

Zhang, Bin, Cunningham, Michael A, Nichols, William C, Bernat, John A, Seligsohn, Uri, Pipe, Steven W, McVey, John H, Schulte-Overberg, Ursula, de Bosch, Norma B, Ruiz-Saez, Arlette, White, Gilbert C., Tuddenham, EGD, Kaufman, Randal J., Ginsburg, David·2003·Nature Genetics

DOI 10.1038/ng1153

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Abstract

Mutations in LMAN1 (also called ERGIC-53) result in combined deficiency of factor V and factor VIII (F5F8D), an autosomal recessive bleeding disorder characterized by coordinate reduction of both clotting proteins. LMAN1 is a mannose-binding type 1 transmembrane protein localized to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC; refs. 2,3), suggesting that F5F8D could result from a defect in secretion of factor V and factor VIII (ref. 4). Correctly folded proteins destined for secretion are packaged in the ER into COPII-coated vesicles, which subsequently fuse to form the ERGIC. Secretion of certain abundant proteins suggests a default pathway requiring no export signals (bulk flow; refs. 6,7). An alternative mechanism involves selective packaging of secreted proteins with the help of specific cargo receptors. The latter model would be consistent with mutations in LMAN1 causing a selective block to export of factor V and factor VIII. But approximately 30% of individuals with F5F8D have normal levels of LMAN1, suggesting that mutations in another gene may also be associated with F5F8D. Here we show that inactivating mutations in MCFD2 cause F5F8D with a phenotype indistinguishable from that caused by mutations in LMAN1. MCFD2 is localized to the ERGIC through a direct, calcium-dependent interaction with LMAN1. These findings suggest that the MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.

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Authors: Zhang, B., Cunningham, M. A., Nichols, W. C., Bernat, J. A., Seligsohn, U., Pipe, S. W., McVey, J. H., Schulte-Overberg, U., de Bosch, N. B., Ruiz-Saez, A., White, G. C., Tuddenham, E., Kaufman, R. J., & Ginsburg, D.
Affiliations: University of Michigan (US)
Cincinnati Children's Hospital Medical Center (US)
Sheba Medical Center (IL)
Imperial College London (GB)
Humboldt-Universität zu Berlin (DE)
University of North Carolina at Chapel Hill (US)
Howard Hughes Medical Institute (US)
Corresponding author: Ginsburg, David
ORCID: Zhang, Bin
Nichols, William C
Bernat, John A
Pipe, Steven W
McVey, John H
Kaufman, Randal J.
Ginsburg, David
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 2003-04-28
Volume: 34
Issue: 2
Pages: 220-225
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/ng1153
OpenAlex: W2085006382
Cited by: 309
References: 29
Citations by year: 2026: 3 · 2025: 5 · 2024: 11 · 2023: 6 · 2022: 11 · 2021: 6 · 2020: 12 · 2019: 7 · 2018: 8 · 2017: 4 · 2016: 5 · 2015: 8 · 2014: 19 · 2013: 18 · 2012: 15
FWCI: 8.63
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
Open Research (University of Surrey) (submittedVersion)
UCL Discovery (University College London) (submittedVersion)
Surrey Research Insight Open Access (The University of Surrey) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Health Sciences › Medicine › Hematology › Hemophilia Treatment and Research
Health Sciences › Medicine › Hematology › Platelet Disorders and Treatments
Keywords: LMAN1, MCFD2, ERGIC-53, factor V deficiency, hemophilia A, bleeding disorders, ER-Golgi transport, cargo receptors, ERGIC, COPII vesicles, calcium-dependent protein interaction, autosomal recessive inheritance
MeSH terms: Amino Acid Sequence, Biological Transport, Active, Carrier Proteins, Endoplasmic Reticulum, Factor V Deficiency, Female, Golgi Apparatus, HeLa Cells, Hemophilia A, Hemorrhage, Humans, Male, Membrane Proteins, Molecular Sequence Data, Mutation, Pedigree, Transfection, Sequence Homology, Amino Acid, Vesicular Transport Proteins, Mannose-Binding Lectins

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Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex

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