Recruitment of UBPY and ESCRT Exchange Drive HD-PTP-Dependent Sorting of EGFR to the MVB

Ali, Nazim; Zhang, Ling; Taylor, Sandra; Mironov, Aleksandr; Urbé, Sylvie; Woodman, Philip

doi:10.1016/j.cub.2013.02.033

Cited by 102 publications

(166 citation statements)

References 50 publications

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“…These include Tom1, Tom1L1, and GGA3, which bind clathrin, Ub, and ESCRT-I supporting the idea that several ESCRT-0-like complexes gather Ub cargo and pass it to a central ESCRT-I/-II supercomplex (Shields and Piper 2011;Haglund and Dikic 2012). Recently, other contenders for Ub-sorting receptors have been identified including Bro1, Alix, and HD-PTP, which bind Ub, and interact with ESCRT-I and ESCRT-III (Ali et al 2013;Pashkova et al 2013). These proteins could potentially offer an additional sorting pathway for Ub cargo in parallel with ESCRT-0.…”

Section: Sequential Orchestration Of Escrt Functionmentioning

confidence: 99%

Ubiquitin-Dependent Sorting in Endocytosis

Piper

Đikić

Lukacs

2014

Cold Spring Harbor Perspectives in Biology

183

176

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When ubiquitin (Ub) is attached to membrane proteins on the plasma membrane, it directs them through a series of sorting steps that culminate in their delivery to the lumen of the lysosome where they undergo complete proteolysis. Ubiquitin is recognized by a series of complexes that operate at a number of vesicle transport steps. Ubiquitin serves as a sorting signal for internalization at the plasma membrane and is the major signal for incorporation into intraluminal vesicles of multivesicular late endosomes. The sorting machineries that catalyze these steps can bind Ub via a variety of Ub-binding domains. At the same time, many of these complexes are themselves ubiquitinated, thus providing a plethora of potential mechanisms to regulate their activity. Here we provide an overview of how membrane proteins are selected for ubiquitination and deubiquitination within the endocytic pathway and how that ubiquitin signal is interpreted by endocytic sorting machineries. HOW PROTEINS ARE SELECTED FOR UBIQUITINATIONU biquitin (Ub) is covalently attached to substrate proteins by the concerted action of E2-conjugating enzymes and E3 ligases (Varshavsky 2012). Most of the specificity and regulation of ubiquitination is at the level of the E3 ligases, which vastly outnumber the E2-conjugating enzymes. Ubiquitination results from the transfer of Ub, held either by the E2 or in some cases by the E3 as a high-energy thioester bond, onto a substrate protein, typically on the terminal amide of a substrate acceptor lysine side chain. Owing to the intense interest in the ubiquitination system, many of the simple rules and distinctions concerning different types of ligases, their specificity for forming particular polyUb chains, and even the kinds of residues in substrate proteins that can be ubiquitin modified, have been blurred with the discovery of mixed poly-Ub chains, new enzymatic mechanisms for Ub transfer, and ubiquitination of nonlysine residues (Kulathu and Komander 2012;Wenzel and Klevit 2012;McDowell and Philpott 2013). Nonetheless, in basic terms, Ub ligases function as platforms that coordinate substrate recognition with Ub transfer as well as configuring poly-Ub chain topology by the E2-conjugating enzyme. Substrates can be bound directly by the E3 ligase or by adaptor proteins that in turn bind to ligases, and selecEditors:

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Section: Sequential Orchestration Of Escrt Functionmentioning

confidence: 99%

Ubiquitin-Dependent Sorting in Endocytosis

Piper

Đikić

Lukacs

2014

Cold Spring Harbor Perspectives in Biology

183

176

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“…Several proteins structurally related to ESCRT-0, including TOM1, have been suggested to be a substitute Ub-cargo receptor to ESCRT-0 (Puertollano, 2005;Shields & Piper, 2011). Recently, other candidates for K63 polyubiquitinated cargo receptors have been identified and include BRO1 in yeast or ALIX in mammals, which both bind Ub, and interact with ESCRT-I and ESCRT-III (Ali et al, 2013;Pashkova et al, 2013). UBDs showing specificity for K63 polyUb chains are also found in ESCRT-I and ESCRT-II subunits, presumably permitting the transmission of the ubiquitinated cargo during the sorting process (Shields & Piper, 2011).…”

Section: Dual Role Of K63-linked Chains In Plant Endocytosismentioning

confidence: 99%

Proteasome‐independent functions of lysine‐63 polyubiquitination in plants

Romero-Barrios

Vert

2017

New Phytologist

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Contents Summary995I.Introduction995II.The plant Ub machinery996III.From Ub to Ub linkage types in plants997IV.Increasing analytical resolution for K63 polyUb in plants998V.How to build K63 polyUb chains?998VI.Cellular roles of K63 polyUb in plants999VII.Physiological roles of K63 polyUb in plants1004VIII.Future perspectives: towards the next level of the Ub code1006Acknowledgements1006References1007 Summary Ubiquitination is a post‐translational modification essential for the regulation of eukaryotic proteins, having an impact on protein fate, function, localization or activity. What originally appeared to be a simple system to regulate protein turnover by the 26S proteasome is now known to be the most intricate regulatory process cells have evolved. Ubiquitin can be arranged in countless chain assemblies, triggering various cellular outcomes. Polyubiquitin chains using lysine‐63 from ubiquitin represent the second most abundant type of ubiquitin modification. Recent studies have exposed their common function in proteasome‐independent functions in non‐plant model organisms. The existence of lysine‐63 polyubiquitination in plants is, however, only just emerging. In this review, we discuss the recent advances on the characterization of ubiquitin chains and the molecular mechanisms driving the formation of lysine‐63‐linked ubiquitin modifications. We provide an overview of the roles associated with lysine‐63 polyubiquitination in plant cells in the light of what is known in non‐plant models. Finally, we review the crucial roles of lysine‐63 polyubiquitin‐dependent processes in plant growth, development and responses to environmental conditions.

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“…Indeed, how ubiquitinated cargoes are initially captured, sequestered, and loaded into vesicles by ESCRTs requires additional study. Recent work shows that EGF receptors are transferred from ESCRT-0 to ESCRT-III by the coordinated action of HD-PTP/PTPN23 and UBPY (Ali et al 2013). This implies a "hand-off " in which cargoes are simultaneously deubiquitinated and loaded into forming vesicles, and should be investigated further.…”

Section: Concluding Remarks: Remaining Questions and Future Studiesmentioning

confidence: 99%

Molecular Mechanisms of the Membrane Sculpting ESCRT Pathway

Henne

Stenmark

Emr

2013

Cold Spring Harbor Perspectives in Biology

382

313

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The endosomal sorting complexes required for transport (ESCRT) drive multivesicular body (MVB) biogenesis and cytokinetic abscission. Originally identified through genetics and cell biology, more recent work has begun to elucidate the molecular mechanisms of ESCRTmediated membrane remodeling, with special focus on the ESCRT-III complex. In particular, several light and electron microscopic studies provide high-resolution imaging of ESCRT-III rings and spirals that purportedly drive MVB morphogenesis and abscission. These studies highlight unifying principles to ESCRT-III function, in particular: (1) the ordered assembly of the ESCRT-III monomers into a heteropolymer, (2) ESCRT-III as a dynamic complex, and (3) the role of the AAA ATPase Vps4 as a contributing factor in membrane scission. Mechanistic comparisons of ESCRT-III function in MVB morphogenesis and cytokinesis suggest common mechanisms in membrane remodeling. THE ESCRT PATHWAY IN MVB BIOGENESIS AND CYTOKINESIS

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Recruitment of UBPY and ESCRT Exchange Drive HD-PTP-Dependent Sorting of EGFR to the MVB

Cited by 102 publications

References 50 publications

Ubiquitin-Dependent Sorting in Endocytosis

Ubiquitin-Dependent Sorting in Endocytosis

Proteasome‐independent functions of lysine‐63 polyubiquitination in plants

Molecular Mechanisms of the Membrane Sculpting ESCRT Pathway

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