Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body

Markus Babst; David J. Katzmann; William B. Snyder; Beverly Wendland; Scott D. Emr

doi:10.1016/S1534-5807(02)00219-8

Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body

Markus Babst, David J. Katzmann, William B. Snyder, Beverly Wendland, Scott D. Emr

Biochemistry and Molecular Biology

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

493 Scopus citations

Abstract

Sorting of ubiquitinated endosomal membrane proteins into the MVB pathway is executed by the class E Vps protein complexes ESCRT-I, -II, and -III, and the AAA-type ATPase Vps4. This study characterizes ESCRT-II, a soluble ∼155 kDa protein complex formed by the class E Vps proteins Vps22, Vps25, and Vps36. This protein complex transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo. We propose that the ESCRT complexes perform a coordinated cascade of events to select and sort MVB cargoes for delivery to the lumen of the vacuole/lysosome.

Original language	English (US)
Pages (from-to)	283-289
Number of pages	7
Journal	Developmental Cell
Volume	3
Issue number	2
DOIs	https://doi.org/10.1016/S1534-5807(02)00219-8
State	Published - Aug 2002

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology
Developmental Biology
Cell Biology

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title = "Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body",

abstract = "Sorting of ubiquitinated endosomal membrane proteins into the MVB pathway is executed by the class E Vps protein complexes ESCRT-I, -II, and -III, and the AAA-type ATPase Vps4. This study characterizes ESCRT-II, a soluble ∼155 kDa protein complex formed by the class E Vps proteins Vps22, Vps25, and Vps36. This protein complex transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo. We propose that the ESCRT complexes perform a coordinated cascade of events to select and sort MVB cargoes for delivery to the lumen of the vacuole/lysosome.",

author = "Markus Babst and Katzmann, {David J.} and Snyder, {William B.} and Beverly Wendland and Emr, {Scott D.}",

note = "Funding Information: We wish to thank Eden Estepa-Sabal for technical support. We also wish to thank Drs. Chris Stefan and Tamara Darsow for critical reading of the manuscript and members of the Emr lab for constructive comments. Thanks to Drs. Joan and Ron Conaway for sharing results prior to their publication. 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)00219-8",

language = "English (US)",

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AU - Babst, Markus

AU - Katzmann, David J.

AU - Snyder, William B.

AU - Wendland, Beverly

AU - Emr, Scott D.

N1 - Funding Information: We wish to thank Eden Estepa-Sabal for technical support. We also wish to thank Drs. Chris Stefan and Tamara Darsow for critical reading of the manuscript and members of the Emr lab for constructive comments. Thanks to Drs. Joan and Ron Conaway for sharing results prior to their publication. 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 - Sorting of ubiquitinated endosomal membrane proteins into the MVB pathway is executed by the class E Vps protein complexes ESCRT-I, -II, and -III, and the AAA-type ATPase Vps4. This study characterizes ESCRT-II, a soluble ∼155 kDa protein complex formed by the class E Vps proteins Vps22, Vps25, and Vps36. This protein complex transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo. We propose that the ESCRT complexes perform a coordinated cascade of events to select and sort MVB cargoes for delivery to the lumen of the vacuole/lysosome.

AB - Sorting of ubiquitinated endosomal membrane proteins into the MVB pathway is executed by the class E Vps protein complexes ESCRT-I, -II, and -III, and the AAA-type ATPase Vps4. This study characterizes ESCRT-II, a soluble ∼155 kDa protein complex formed by the class E Vps proteins Vps22, Vps25, and Vps36. This protein complex transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo. We propose that the ESCRT complexes perform a coordinated cascade of events to select and sort MVB cargoes for delivery to the lumen of the vacuole/lysosome.

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Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body

Abstract

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