ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting

Markus Babst; David J. Katzmann; Eden J. Estepa-Sabal; Timo Meerloo; Scott D. Emr

doi:10.1016/S1534-5807(02)00220-4

ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting

Markus Babst, David J. Katzmann, Eden J. Estepa-Sabal, Timo Meerloo, Scott D. Emr

Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › peer-review

632 Scopus citations

Abstract

The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.

Original language	English (US)
Pages (from-to)	271-282
Number of pages	12
Journal	Developmental Cell
Volume	3
Issue number	2
DOIs	https://doi.org/10.1016/S1534-5807(02)00220-4
State	Published - Aug 2002

ASJC Scopus subject areas

Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Developmental Biology
Cell Biology

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10.1016/S1534-5807(02)00220-4

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title = "ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting",

abstract = "The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.",

author = "Markus Babst and Katzmann, {David J.} and Estepa-Sabal, {Eden J.} and Timo Meerloo and Emr, {Scott D.}",

note = "Funding Information: We wish to thank Drs. Chris Stefan and Tamara Darsow for critical reading of the manuscript and members of the Emr lab for constructive comments. We would also like to thank Dr. Marian Carlson for useful discussions. T.M. is a member of Immunoelectron Microscopy core B, program project grant CA58689, headed by M. Farquhar. This work was supported by a grant from the NIH to S.D.E. (CA58689), a fellowship from the Howard Hughes Medical Institute (M.B.), and a fellowship from the American Cancer Society (D.J.K.). S.D.E. is supported as an Investigator of the Howard Hughes Medical Institute.",

year = "2002",

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doi = "10.1016/S1534-5807(02)00220-4",

language = "English (US)",

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journal = "Developmental Cell",

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T2 - An endosome-associated heterooligomeric protein complex required for MVB sorting

AU - Babst, Markus

AU - Katzmann, David J.

AU - Estepa-Sabal, Eden J.

AU - Meerloo, Timo

AU - Emr, Scott D.

N1 - Funding Information: We wish to thank Drs. Chris Stefan and Tamara Darsow for critical reading of the manuscript and members of the Emr lab for constructive comments. We would also like to thank Dr. Marian Carlson for useful discussions. T.M. is a member of Immunoelectron Microscopy core B, program project grant CA58689, headed by M. Farquhar. This work was supported by a grant from the NIH to S.D.E. (CA58689), a fellowship from the Howard Hughes Medical Institute (M.B.), and a fellowship from the American Cancer Society (D.J.K.). S.D.E. is supported as an Investigator of the Howard Hughes Medical Institute.

PY - 2002/8

Y1 - 2002/8

N2 - The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.

AB - The sorting of transmembrane proteins (e.g., cell surface receptors) into the multivesicular body (MVB) pathway to the lysosomal/vacuolar lumen requires the function of the ESCRT protein complexes. The soluble coiled-coil-containing proteins Vps2, Vps20, Vps24, and Snf7 are recruited from the cytoplasm to endosomal membranes where they oligomerize into a protein complex, ESCRT-III. ESCRT-III contains two functionally distinct subcomplexes. The Vps20-Snf7 subcomplex binds to the endosomal membrane, in part via the myristoyl group of Vps20. The Vps2-Vps24 subcomplex binds to the Vps20-Snf7 complex and thereby serves to recruit additional cofactors to this site of protein sorting. We provide evidence for a role for ESCRT-III in sorting and/or concentration of MVB cargoes.

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ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting

Abstract

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