How Ubiquitin Functions with ESCRTs

Shields, S. Brookhart; Piper, Robert C.

doi:10.1111/j.1600-0854.2011.01242.x

Cited by 150 publications

(177 citation statements)

References 179 publications

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“…4 endosomal sorting complex and is required for the transport (ESCRTs) machinery that includes ESCRT-0, ESCRT-I, ESCRT-II and ESCRT-III complexes and is subsequently sequestered into vacuoles/lysosomes for degradation by luminal proteases (Henne et al, 2013;Shields and Piper, 2011). Although homologs of most ESCRT 0-III complex components occurring in yeast and mammals are found in the Arabidopsis genome (Barberon et al, 2014;Hurley and Emr, 2006), the functions of only a few of these homologs have been explored.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Lou

Tian

et al. 2016

Molecular Plant

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.All studies published in MOLECULAR PLANT are embargoed until 3PM ET of the day they are published as corrected proofs on-line. Studies cannot be publicized as accepted manuscripts or uncorrected proofs. proteasome system, which strengthens our understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling. proteasome system, further strengthen our understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling. M A N U S C R I P T A C C E P T E D

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Section: Accepted Manuscriptmentioning

confidence: 99%

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Lou

Tian

et al. 2016

Molecular Plant

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“…Lysosomal degradation of membrane proteins is mediated by their attachment to ubiquitin (Ub), which serves as a sorting tag for entry into intralumenal vesicles (ILVs) that bud from the limiting membrane of endosomes [1][2][3]. The ILVs accumulate in late endosomes/multivesicular bodies (MVBs), which fuse to lysosomes and thereby deliver ubiquitinated, vesicle-incorporated membrane proteins to the lysosome lumen for degradation.…”

Section: Introductionmentioning

confidence: 99%

Cargo ubiquitination is essential for multivesicular body intralumenal vesicle formation

et al. 2012

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The efficient formation of a variety of transport vesicles is influenced by the presence of cargo, suggesting that cargo itself might have a defining role in vesicle biogenesis. However, definitive in vivo experiments supporting this concept are lacking, as it is difficult to eliminate endogenous cargo. The Endosomal Sorting Complexes Required for Transport (ESCRT) apparatus sorts ubiquitinated membrane proteins into endosomal intralumenal vesicles (ILVs) that accumulate within multivesicular bodies. Here we show that cargo ubiquitination is required for effective recruitment of the ESCRT machinery onto endosomal membranes and for the subsequent formation of ILVs.

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“…For the most part, mono-Ub and K63-linked chains predominate in the endocytic pathway as sorting signals when attached to cargo proteins, although other linkages such as K11, K29, and K48 may be operational as well (Shields and Piper 2011). In experimental settings, namely, where Ub is permanently attached cargo, a single Ub is sufficient for delivery to lysosomes (Shih et al 2000;Raiborg et al 2002;Stringer and Piper 2011).…”

Section: Ubiquitin-dependent Sorting In Endocytosismentioning

confidence: 99%

“…ESCRT-0 has a number of biochemical features that allow it to function as the initial receptor for Ub cargo (Shields and Piper 2011). First, it has several UBDs: one within each of its two amino-terminal VHS domains, three UIMs found in the middle of both proteins, and an additional UBD within the SH3 domain of STAM2 (Lange et al 2012a).…”

Section: Ubiquitin-dependent Sorting In Endocytosismentioning

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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How Ubiquitin Functions with ESCRTs

Cited by 150 publications

References 179 publications

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Cargo ubiquitination is essential for multivesicular body intralumenal vesicle formation

Ubiquitin-Dependent Sorting in Endocytosis

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