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ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting.

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.

SUBMITTER: Shields SB

PROVIDER: S-EPMC2700381 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting.

Shields S Brookhart SB Oestreich Andrea J AJ Winistorfer Stanley S Nguyen Doris D Payne Johanna A JA Katzmann David J DJ Piper Robert R

The Journal of cell biology 20090401 2

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 ...[more]

PMID: 19380877

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