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ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting

Shields, S. Brookhart, Oestreich, Andrea J., Winistorfer, Stanley, Nguyen, Doris, Payne, Johanna A., Katzmann, David J., Piper, Robert·2009·Journal of Cell Biology
DOI 10.1083/jcb.200811130PMC PMC2700381
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Abstract

Ubiquitin (Ub) sorting receptors facilitate the targeting of ubiquitinated membrane proteins into multivesicular bodies (MVBs). Ub-binding domains (UBDs) have been described in several endosomal sorting complexes required for transport (ESCRT). Using available structural information, we have investigated the role of the multiple UBDs within ESCRTs during MVB cargo selection. We found a novel UBD within ESCRT-I and show that it contributes to MVB sorting in concert with the known UBDs within the ESCRT complexes. These experiments reveal an unexpected level of coordination among the ESCRT UBDs, suggesting that they collectively recognize a diverse set of cargo rather than act sequentially at discrete steps.

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  • The ESCRT complex interacts with proteins carrying P(S/T)AP and/or PPXY motifs; P(S/T)AP binds TSG101, which binds ALIX, while NEDD4-E3 ligases recruited via PPXY motifs and subsequent ubiquitination facilitate ESCRT recruitment.

    “It is well established that the ESCRT complex interacts with proteins carrying P(S/T)AP and/or PPXY motifs. The P(S/T)AP domain binds to TSG101, which in turn binds ALIX20, while recruitment of NEDD4-E3 ligases via PPXY motifs, and subsequent protein ubiquitination, further facilitates the recruitment of the ESCRT machinery21.”

    From TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress (2024) · cites this paper as [21]

    The Introduction describes ESCRT components binding ubiquitinated cargo, supporting the general link between ubiquitination and ESCRT-mediated sorting. The Results and discussion also note that TSG101 interacts with PTAP motifs. Our copy does not describe PPXY-mediated recruitment of NEDD4-E3 ligases or TSG101 binding ALIX, so it does not support the claimed interaction chain. (LLM, conf=0.86)

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Research works printed but not linked: 37

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Metadata

Authors
Shields, S. B., Oestreich, A. J., Winistorfer, S., Nguyen, D., Payne, J. A., Katzmann, D. J., & Piper, R.
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2009-04-20
Volume
185
Issue
2
Pages
213-224
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.200811130
PMC
PMC2700381
Cited by
101
References
1
Language
en

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