Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery

Carlton, Jeremy G.; Martín-Serrano, Juan

doi:10.1126/science.1143422

Cited by 677 publications

(844 citation statements)

References 26 publications

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“…Microtubule-associated proteins PRC1 [13,14] Centralspindlin complex CYK-4 [2,15] MKLP1 [2,15] Chromosome passenger complex INCENP [16,17] Survinin [16,17] Borealin [16,17] Aurora B [16,17] ESRCTs and associated proteins CEP55 [30][31][32] TSG101 [31,32] ALIX [31,32] CHMP1B [33] Spastin [33] CHMP4B [31,32,34] FYVE-CENT [34] TTC19 [34] Kinesins KIF4A [14] MKLP2 [17] MPP1 [22] KIF14 [23] KIF13A [34] Additional proteins NuSAP [18] Orbit [19] ASP [20] TBCD [21] ECT2 [24] FIP3 [25] PLK1 [26,27] Septins [28] Anillin [29] during anaphase and cytokinesis and is important for the last step of abscission. CEP55 binds directly MKLP1 and is controlled by centralspindlin, since knockdown of centralspindlin abolishes CEP55 from the midbody [30].…”

Section: The Abscission Step Of Cytokinesismentioning

confidence: 99%

Cytokinesis and cancer

Sagona

Stenmark

2010

FEBS Letters

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a b s t r a c tCytokinesis is the final stage of cell division during which the two daughter cells separate completely. Although less well understood than some of the earlier phases of the cell cycle, recent discoveries have shed light on the mechanisms that orchestrate this process, including cleavage furrow formation, midbody maturation and abscission. One of the reasons why research on cytokinesis has been attracting increasing attention is the concept that failure of this process in mammals is associated with carcinogenesis. In this minireview, we will discuss the possible links between cytokinesis and cancer, and highlight key mechanisms that connect these processes.

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Section: The Abscission Step Of Cytokinesismentioning

confidence: 99%

Cytokinesis and cancer

Sagona

Stenmark

2010

FEBS Letters

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“…In eukaryotic cells, the MVB pathway controls various important processes such as receptor down-regulation, antigen presentation, cytokinesis, retroviral budding, and autophagy (1)(2)(3)(4)(5)(6). In the budding yeast Saccharomyces cerevisiae, previous studies identified a number of genes involved in vacuolar protein sorting (VPS) (7,8).…”

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confidence: 99%

The Endosomal Na+/H+ Exchanger Contributes to Multivesicular Body Formation by Regulating the Recruitment of ESCRT-0 Vps27p to the Endosomal Membrane

Mitsui

Koshimura

Yoshikawa

et al. 2011

Journal of Biological Chemistry

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Multivesicular bodies (MVBs) are late endosomal compartments containing luminal vesicles (MVB vesicles) that are formed by inward budding of the endosomal membrane. In budding yeast, MVBs are an important cellular mechanism for the transport of membrane proteins to the vacuolar lumen. This process requires a class E subset of vacuolar protein sorting (VPS) genes. VPS44 (allelic to NHX1) encodes an endosomelocalized Na ؉ /H ؉ exchanger. The function of the VPS44 exchanger in the context of vacuolar protein transport is largely unknown. Using a cell-free MVB formation assay system, we demonstrated that Nhx1p is required for the efficient formation of MVB vesicles in the late endosome. The recruitment of Vps27p, a class E Vps protein, to the endosomal membrane was dependent on Nhx1p activity and was enhanced by an acidic pH at the endosomal surface. Taken together, we propose that Nhx1p contributes to MVB formation by the recruitment of Vps27p to the endosomal membrane, possibly through Nhx1p antiporter activity.Multivesicular bodies (MVBs) 3 are a subset of late endosomes that contain internal vesicles, permitting precursor and plasma membrane proteins to reach the lysosome or vacuole lumen for degradation or maturation, respectively. In eukaryotic cells, the MVB pathway controls various important processes such as receptor down-regulation, antigen presentation, cytokinesis, retroviral budding, and autophagy (1-6). In the budding yeast Saccharomyces cerevisiae, previous studies identified a number of genes involved in vacuolar protein sorting (VPS) (7,8). These Vps proteins function at distinct steps of protein transport between the Golgi complex and the vacuole (7,8). A subset of Vps proteins, class E proteins, is involved in MVB formation. Most class E proteins are components of five distinct complexes; Vps27p-Hse1p (also called endosomal sorting complexes required for transport-0 (ESCRT-0), -I, -II, and -III and Vps4p. These complexes are required for the formation of internal vesicles and sorting of cargo proteins to the vesicles from the endosomal membrane (3, 9). Vps27p (ESCRT-0) recruits ESCRT-I, which in turn recruits and/or activates ESCRT-II and ESCRT-III at the endosome (3, 10). Recent in vitro studies have provided new insights into the precise role of each ESCRT complex in MVB formation (11-13). ESCRT-0 initiates the MVB sorting process by recruiting ESCRT-I to the endosomal membrane and concentrating ubiquitylated MVB cargos to the vesicle budding site (12). ESCRT-I and ESCRT-II are directly involved in membrane budding by stabilizing the bud necks, whereas ESCRT-III is responsible for the cleavage of bud necks (11-13). Finally, the AAA-type ATPase Vps4p dissociates the ESCRT-III complex from the endosome (14). The sequential activity of these complexes on the cytoplasmic surface of endosomes directs the budding and fission of vesicles into the lumen of the endosome and the sequestration of cargo proteins in the vesicle. Defects in ESCRT proteins prevent internal vesicle formation and result in exagg...

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“…Among the four multi-subunit protein complexes (ESCRT 0-I-II-III), extensive studies reported the fundamental role of ESCRT-III in abscission (Capalbo et al, 2016;Carlton et al, 2012;Carlton and Martin-Serrano, 2007;Eikenes et al, 2015;Lafaurie-Janvore et al, 2013;Morita et al, 2007). ESCRT-III becomes enriched at the midbody, an organelle at the intercellular bridge, which acts as a platform for the recruitment and organisation of various proteins involved in both the control and execution of the abscission process.…”

Section: Escrt and Ptdins3p: Potential Connections And Future Directimentioning

confidence: 99%

Cytokinetic Abscission: Phosphoinositides and ESCRTs Direct the Final Cut

Gulluni

Martini

Hirsch

2017

J of Cellular Biochemistry

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Cytokinetic abscission involves the fine and regulated recruitment of membrane remodeling proteins that participate in the abscission of the intracellular bridge that connects the two dividing cells. This essential process is mediated by the concomitant activity of the endosomal sorting complex required for transport (ESCRT) and the vesicular trafficking directed to the midbody.Phosphoinositides (PtdIns), produced at plasma membrane and endosomes, act as molecular intermediates by recruiting effector proteins involved in multiple cellular processes, such as intracellular signalling, endo-and exo-cytosis and membrane remodelling events. Emerging evidences suggest that PtdIns have an active role in recruiting key elements that control the stability and the remodelling of the cytoskeleton from the furrow ingression to the abscission, at the end of cytokinesis. Accordingly, a possible concomitant and coordinated activity between PtdIns production and ESCRT machinery assembly could also exist and recent findings are pointing the attention on poorly understood ESCRT subunits potentially able to associate with PtdIns rich membranes. Although further studies are required to link PtdIns to ESCRT machinery during abscission, this might represent a promising field of study.

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Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery

Cited by 677 publications

References 26 publications

Cytokinesis and cancer

Cytokinesis and cancer

The Endosomal Na+/H+ Exchanger Contributes to Multivesicular Body Formation by Regulating the Recruitment of ESCRT-0 Vps27p to the Endosomal Membrane

Cytokinetic Abscission: Phosphoinositides and ESCRTs Direct the Final Cut

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