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The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans

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The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. / Liégeois, Samuel; Benedetto, Alexandre; Garnier, Jean-Marie et al.
In: Journal of Cell Biology, Vol. 173, No. 6, 19.06.2006, p. 949-961.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Liégeois, S, Benedetto, A, Garnier, J-M, Schwab, Y & Labouesse, M 2006, 'The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans', Journal of Cell Biology, vol. 173, no. 6, pp. 949-961. https://doi.org/10.1083/jcb.200511072

APA

Vancouver

Liégeois S, Benedetto A, Garnier J-M, Schwab Y, Labouesse M. The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. Journal of Cell Biology. 2006 Jun 19;173(6):949-961. doi: 10.1083/jcb.200511072

Author

Liégeois, Samuel ; Benedetto, Alexandre ; Garnier, Jean-Marie et al. / The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. In: Journal of Cell Biology. 2006 ; Vol. 173, No. 6. pp. 949-961.

Bibtex

@article{848a9a4f44e4482a9a0372109f09ff76,
title = "The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans",
abstract = "Polarized intracellular trafficking in epithelia is critical in development, immunity, and physiology to deliver morphogens, defensins, or ion pumps to the appropriate membrane domain. The mechanisms that control apical trafficking remain poorly defined. Using Caenorhabditis elegans, we characterize a novel apical secretion pathway involving multivesicularbodies and the release of exosomes at the apical plasma membrane. By means of two different genetic approaches, we show that the membrane-bound V0 sector of the vacuolar H+-ATPase (V-ATPase) acts in this pathway, independent of its contribution to the V-ATPase proton pump activity. Specifically, we identified mutations in the V0 {"}a{"} subunit VHA-5 that affect either the V0-specific function or the V0+V1 function of the V-ATPase. These mutations allowed us to establish that the V0 sector mediates secretion of Hedgehog-related proteins. Our data raise the possibility that the V0 sector mediates exosome and morphogen release in mammals.",
keywords = "Amino Acid Sequence, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Hedgehog Proteins, Models, Biological, Molecular Sequence Data, Mutagenesis, Site-Directed, Phenotype, Protein Structure, Tertiary, Protein Transport, Secretory Vesicles, Sequence Alignment, Trans-Activators, Vacuolar Proton-Translocating ATPases, Journal Article, Research Support, Non-U.S. Gov't",
author = "Samuel Li{\'e}geois and Alexandre Benedetto and Jean-Marie Garnier and Yannick Schwab and Michel Labouesse",
year = "2006",
month = jun,
day = "19",
doi = "10.1083/jcb.200511072",
language = "English",
volume = "173",
pages = "949--961",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6",

}

RIS

TY - JOUR

T1 - The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans

AU - Liégeois, Samuel

AU - Benedetto, Alexandre

AU - Garnier, Jean-Marie

AU - Schwab, Yannick

AU - Labouesse, Michel

PY - 2006/6/19

Y1 - 2006/6/19

N2 - Polarized intracellular trafficking in epithelia is critical in development, immunity, and physiology to deliver morphogens, defensins, or ion pumps to the appropriate membrane domain. The mechanisms that control apical trafficking remain poorly defined. Using Caenorhabditis elegans, we characterize a novel apical secretion pathway involving multivesicularbodies and the release of exosomes at the apical plasma membrane. By means of two different genetic approaches, we show that the membrane-bound V0 sector of the vacuolar H+-ATPase (V-ATPase) acts in this pathway, independent of its contribution to the V-ATPase proton pump activity. Specifically, we identified mutations in the V0 "a" subunit VHA-5 that affect either the V0-specific function or the V0+V1 function of the V-ATPase. These mutations allowed us to establish that the V0 sector mediates secretion of Hedgehog-related proteins. Our data raise the possibility that the V0 sector mediates exosome and morphogen release in mammals.

AB - Polarized intracellular trafficking in epithelia is critical in development, immunity, and physiology to deliver morphogens, defensins, or ion pumps to the appropriate membrane domain. The mechanisms that control apical trafficking remain poorly defined. Using Caenorhabditis elegans, we characterize a novel apical secretion pathway involving multivesicularbodies and the release of exosomes at the apical plasma membrane. By means of two different genetic approaches, we show that the membrane-bound V0 sector of the vacuolar H+-ATPase (V-ATPase) acts in this pathway, independent of its contribution to the V-ATPase proton pump activity. Specifically, we identified mutations in the V0 "a" subunit VHA-5 that affect either the V0-specific function or the V0+V1 function of the V-ATPase. These mutations allowed us to establish that the V0 sector mediates secretion of Hedgehog-related proteins. Our data raise the possibility that the V0 sector mediates exosome and morphogen release in mammals.

KW - Amino Acid Sequence

KW - Animals

KW - Caenorhabditis elegans

KW - Caenorhabditis elegans Proteins

KW - Hedgehog Proteins

KW - Models, Biological

KW - Molecular Sequence Data

KW - Mutagenesis, Site-Directed

KW - Phenotype

KW - Protein Structure, Tertiary

KW - Protein Transport

KW - Secretory Vesicles

KW - Sequence Alignment

KW - Trans-Activators

KW - Vacuolar Proton-Translocating ATPases

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1083/jcb.200511072

DO - 10.1083/jcb.200511072

M3 - Journal article

C2 - 16785323

VL - 173

SP - 949

EP - 961

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 6

ER -