Escrt-III

Babst, Markus; Katzmann, David J.; Estepa-Sabal, Eden J.; Meerloo, Timo; Emr, Scott D.

doi:10.1016/s1534-5807(02)00220-4

Cited by 809 publications

(360 citation statements)

References 34 publications

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“…Vps4p has been shown to interact with both Vta1p and the ESCRT-III protein Vps20p by in vivo and in vitro analysis (19,24). ESCRT-III is composed of two subcomplexes, the Vps2p-Vps24p subcomplex and the Vps20p-Vps32p subcomplex (15). Data obtained from our yeast two-hybrid analysis of the class E Vps proteins identified an interaction between Vta1p and Vps32p (ESCRT-III).…”

Section: Vps46pmentioning

confidence: 95%

“…The model for sorting at the late endosome includes ubiquitinated protein cargo first binding ESCRT-0 and -I being recruited to the membrane, followed by the recruitment of ESCRT-II and -III to the endosomal membrane. The protein cargo is deubiquitinated by the enzyme Doa4p, whereas the AAA-type ATPase (ATPase associated with a variety of cellular activities) Vps4p binds and disassembles the ESCRT-III complex from the membrane (2,6,11,15). Upon ESCRT-III disassociation, the cargo proteins are found in the membrane invaginations of the MVB.…”

mentioning

confidence: 99%

“…In MVB sorting, ESCRT-III complex disassembly and release from the membrane requires the ATPase activity of Vps4p (15,18). The ADP-bound form of Vps4p exists as a dimer and is mainly cytosolic (18).…”

mentioning

confidence: 99%

“…Upon nucleotide exchange, Vps4p assembles into an oligomeric complex that has been shown to contain 10-12 Vps4p monomers (18,19). The ATP-bound complex of Vps4p is localized to the endosomal membrane where it proceeds to catalyze the release of the ESCRT-III protein complex (15,16).…”

mentioning

confidence: 99%

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Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body

Lottridge

Flannery

Vincelli

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

122

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Section: Vps46pmentioning

confidence: 95%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body

Lottridge

Flannery

Vincelli

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

122

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“…Hrs appears to be the first protein to be recruited to endosomes (4 -6) through an interaction of its FIVE domain with phosphatidylinositol 3-phosphate (7), a lipid highly enriched in endosomal membranes (8). This is followed by the consecutive recruitment of three multisubunit complexes termed ESCRT-I (9), ESCRT-II (10), and ESCRT-III (11). Finally, the AAA-type ATPase Vps4 binds ESCRT-III and, following MVB vesicle formation, promotes the dissociation of the ESCRT protein complexes from endosomes for additional rounds of protein sorting (12).…”

mentioning

confidence: 99%

Interactions of TOM1L1 with the Multivesicular Body Sorting Machinery

Puertollano

2005

Journal of Biological Chemistry

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Tom1L1 (Tom1-like1) and related proteins Tom1 (Target of Myb1) and Tom1L2 (Tom1-like2) constitute a new protein family characterized by the presence of a VHS (Vps27p/Hrs/Stam) domain in the N-terminal portion followed by a GAT (GGA and Tom) domain. Recently it was demonstrated that the GAT domain of both Tom1 and Tom1L1 binds ubiquitin, suggesting that these proteins might participate in the sorting of ubiquitinated proteins into multivesicular bodies (MVBs). Here we report a novel interaction between Tom1L1 and members of the MVB sorting machinery. Specifically, we found that the VHS domain of Tom1L1 interacts with Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate), whereas a PTAP motif, located between the VHS and GAT domain of Tom1L1, is responsible for binding to TSG101 (tumor susceptibility gene 101). Myc epitopetagged Tom1L1 showed a cytosolic distribution but was recruited to endosomes following Hrs expression. In addition, Tom1L1 possesses several tyrosine motifs at the C-terminal region that mediate interactions with members of the Src family kinases and other signaling proteins such as Grb2 and p85. We showed that a fraction of Fyn kinase localizes at endosomes and that this distribution becomes more evident after epidermal growth factor internalization. Moreover, expression of a constitutive active form of Fyn also promoted the recruitment of Tom1L1 to enlarged endosomes. Taken together, we propose that Tom1L1 could act as an intermediary between signaling and degradative pathways.Regulated degradation of cell surface proteins, particularly receptors involved in signaling pathways, is essential for the control of many biological processes, including cell proliferation, survival, migration, and differentiation (1, 2). Internalized membrane-protein cargo can be delivered either to recycling vesicles for transport back to the cell surface or to late endosomes for transfer to lysosomes and degradation. Multivesicular bodies (MVBs) 1 are the compartments where this sorting event takes place (3). Thus, proteins to be degraded are included into small vesicles that invaginate into the lumen of the endosome. Subsequent fusion of MVBs with lysosomes releases these vesicles into the lysosome lumen, where they are degraded by lysosomal hydrolases. In contrast, proteins that remain in the limiting membrane of MVBs are recycled to the trans-Golgi network (TGN) or plasma membrane. In the last few years, a number of genetic and biochemical studies have allowed the characterization of the molecular machinery implicated in the formation of MVBs. Hrs appears to be the first protein to be recruited to endosomes (4 -6) through an interaction of its FIVE domain with phosphatidylinositol 3-phosphate (7), a lipid highly enriched in endosomal membranes (8). This is followed by the consecutive recruitment of three multisubunit complexes termed ESCRT-I (9), ESCRT-II (10), and ESCRT-III (11). Finally, the AAA-type ATPase Vps4 binds ESCRT-III and, following MVB vesicle formation, promotes the dissociation of the E...

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Plant endosomes as protein sorting hubs

2022

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Endocytosis, secretion, and endosomal trafficking are key cellular processes that control the composition of the plasma membrane. Through the coordination of these trafficking pathways, cells can adjust the composition, localization, and turnover of proteins and lipids in response to developmental or environmental cues. Upon being incorporated into vesicles and internalized through endocytosis, plant plasma membrane proteins are delivered to the trans-Golgi network (TGN). At the TGN, plasma membrane proteins are recycled back to the plasma membrane or transferred to multivesicular endosomes (MVEs), where they are further sorted into intralumenal vesicles for degradation in the vacuole. Both types of plant endosomes, TGN and MVEs, act as sorting organelles for multiple endocytic, recycling, and secretory pathways. Molecular assemblies such as retromer, ESCRT (endosomal sorting complex required for transport) machinery, small GTPases, adaptor proteins, and SNAREs associate with specific domains of endosomal membranes to mediate different sorting and membrane-budding events. In this review, we discuss the mechanisms underlying the recognition and sorting of proteins at endosomes, membrane remodeling and budding, and their implications for cellular trafficking and physiological responses in plants.

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Escrt-III

Cited by 809 publications

References 34 publications

Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body

Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body

Interactions of TOM1L1 with the Multivesicular Body Sorting Machinery

Plant endosomes as protein sorting hubs

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