Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes (Q24313594)

GOA release 2020-03-11

author

Harald Stenmark

4

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author name string

Kristi G Bache

1

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Andreas Brech

2

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Anja Mehlum

Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates

3

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language of work or name

English

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publication date

4 August 2003

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published in

Journal of Cell Biology

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volume

162

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issue

3

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page(s)

435-42

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cites work

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

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Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I.

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FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes

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EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts

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Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes

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Vps27 recruits ESCRT machinery to endosomes during MVB sorting

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Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking.

27 September 2017

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27 September 2017

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27 September 2017

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A lipid associated with the antiphospholipid syndrome regulates endosome structure and function

27 September 2017

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27 September 2017

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Tsg101: HIV-1's ticket to ride

29 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12900395

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

An ESCRT into the endosome

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12900395

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1083/JCB.200302131

1 reference

2093407

2093407

1 reference

1 reference

1 reference