Interaction of the Mammalian Endosomal Sorting Complex Required for Transport (ESCRT) III Protein hSnf7-1 with Itself, Membranes, and the AAA+ ATPase SKD1

Lin, Yuan; Kimpler, Lisa A.; Naismith, Teresa V.; Lauer, Joshua M.; Hanson, Phyllis I.

doi:10.1074/jbc.m413968200

Cited by 146 publications

(197 citation statements)

References 61 publications

(94 reference statements)

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“…2 A-D). Moreover, under these conditions the fluorescently tagged ESCRT proteins show their expected interphase cytosolic localization (8,20,21), and there is no increase in multinucleated cells, indicating that cytokinesis is not disrupted (Fig. S2).…”

Section: Resultsmentioning

confidence: 97%

Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission

Elia

Sougrat

Spurlin

et al. 2011

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

358

550

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The final stage of cytokinesis is abscission, the cutting of the narrow membrane bridge connecting two daughter cells. The endosomal sorting complex required for transport (ESCRT) machinery is required for cytokinesis, and ESCRT-III has membrane scission activity in vitro, but the role of ESCRTs in abscission has been undefined. Here, we use structured illumination microscopy and timelapse imaging to dissect the behavior of ESCRTs during abscission. Our data reveal that the ESCRT-I subunit tumor-susceptibility gene 101 (TSG101) and the ESCRT-III subunit charged multivesicular body protein 4b (CHMP4B) are sequentially recruited to the center of the intercellular bridge, forming a series of cortical rings. Late in cytokinesis, however, CHMP4B is acutely recruited to the narrow constriction site where abscission occurs. The ESCRT disassembly factor vacuolar protein sorting 4 (VPS4) follows CHMP4B to this site, and cell separation occurs immediately. That arrival of ESCRT-III and VPS4 correlates both spatially and temporally with the abscission event suggests a direct role for these proteins in cytokinetic membrane abscission.

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Section: Resultsmentioning

confidence: 97%

Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission

Elia

Sougrat

Spurlin

et al. 2011

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

358

550

View full text Add to dashboard Cite

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“…6 -8) (53). In most ESCRT-III proteins, the fifth helix and surrounding regions can fold back onto the core domain and make autoinhibitory interactions (12,53,75,76). We found, however, that LIP5(MIT) 2 bound with the same affinity to full-length CHMP5 as to the minimal CHMP5 binding site (Fig.…”

Section: Discussionmentioning

confidence: 99%

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Skalicky¹,

Arii²,

Wenzel³

et al. 2012

Journal of Biological Chemistry

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Background: LIP5 helps regulate the membrane fission and recycling activities of the ESCRT pathway. Results: Biochemical and structural studies reveal how LIP5 binds different ESCRT-III proteins. Conclusion: ESCRT-III proteins bind independently to different LIP5 sites, and the LIP5-CHMP5 structure reveals a novel interaction mode. Significance: The results help explain how LIP5 can activate VPS4 ATPases to act on ESCRT-III filaments.

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“…Expression and Purification of YeSlc26A2 STAS DomainThe YeSlc26A2 STAS domain (amino acids 381-483) was cloned into the pEHISTEV plasmid (15) between the NcoI and XhoI sites using two oligonucleotides: 5Ј-atgcccatggtggcgcatgtgatttatgcagag-3Ј (NcoI site underlined) and 5Ј-atgcctcgagttacctcaaatttccgctgag-3Ј (XhoI site underlined). The protein was overexpressed in E. coli BL21(DE3) cells and purified under the same conditions as the full-length protein except that the detergent was excluded.…”

Section: Methodsmentioning

confidence: 99%

Low Resolution Structure of a Bacterial SLC26 Transporter Reveals Dimeric Stoichiometry and Mobile Intracellular Domains

Compton

Karinou

Naismith

et al. 2011

Journal of Biological Chemistry

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The SLC26/SulP (solute carrier/sulfate transporter) proteins are a superfamily of anion transporters conserved from bacteria to man, of which four have been identified in human diseases. Proteins within the SLC26/SulP family exhibit a wide variety of functions, transporting anions from halides to carboxylic acids. The proteins comprise a transmembrane domain containing between 10 -12 transmembrane helices followed a by C-terminal cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domain. These proteins are expected to undergo conformational changes during the transport cycle; however, structural information for this family remains sparse, particularly for the full-length proteins. To address this issue, we conducted an expression and detergent screen on bacterial Slc26 proteins. The screen identified a Yersinia enterocolitica Slc26A protein as the ideal candidate for further structural studies as it can be purified to homogeneity. Partial proteolysis, co-purification, and analytical size exclusion chromatography demonstrate that the protein purifies as stable oligomers. Using small angle neutron scattering combined with contrast variation, we have determined the first low resolution structure of a bacterial Slc26 protein without spectral contribution from the detergent. The structure confirms that the protein forms a dimer stabilized via its transmembrane core; the cytoplasmic STAS domain projects away from the transmembrane domain and is not involved in dimerization. Supported by additional biochemical data, the structure suggests that large movements of the STAS domain underlie the conformational changes that occur during transport.The SLC26/SulP 4 proteins are a superfamily of anion transporters conserved from bacteria to man (1). The human genome encodes at least 10 SLC26 proteins that play critical roles in cell physiology and are medically important, being implicated in genetic diseases such as diastrophic dysplasia, congenital chloride diarrhea, Pendred syndrome, and nonsyndromic deafness (2, 3). Proteins within the SLC26/SulP family exhibit a wide variety of functions, transporting anions ranging from halides to carboxylic acids. The molecular basis for this diversity, however, is poorly understood and structural information is extremely limited. A model of the transmembrane region containing 12 transmembrane helices has been published for the Synechococcus Slc26 protein BicA, and it has been proposed that this topology may apply across the family (4). A conserved stoichiometry within the family is the subject of debate as several members, across multiple species, have been reported to form dimers and/or tetramers (5-7). The only high resolution structural data available to date is for the cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domain, which is fused to the C terminus of the transmembrane domain (8 -10).SLC26 transporters must undergo sequential conformational changes during the transport cycle as typified by prestin (SLC26A5), the cochlear protein th...

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Interaction of the Mammalian Endosomal Sorting Complex Required for Transport (ESCRT) III Protein hSnf7-1 with Itself, Membranes, and the AAA+ ATPase SKD1

Cited by 146 publications

References 61 publications

Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission

Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission

Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport

Low Resolution Structure of a Bacterial SLC26 Transporter Reveals Dimeric Stoichiometry and Mobile Intracellular Domains

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