Results 51 to 60 of about 14,499 (192)

Femtoliter Injection of ESCRT-III Proteins into Adhered Giant Unilamellar Vesicles

open access: yesBio-Protocol, 2022
The endosomal sorting complex required for transport (ESCRT) machinery mediates membrane fission reactions that exhibit a different topology from that observed in clathrin-coated vesicles.
Vasil Georgiev   +3 more
doaj   +1 more source

ESCRT-III has an escort [PDF]

open access: yesJournal of Cell Biology, 2011
![Figure][1] More intralumenal vesicles (red) break away from the endosome membrane in control cells (left) than in cells that overexpress a domain of Bro1 (right). The protein Bro1 lives up to its name, [Wemmer et al.][2] show.
openaire   +1 more source

Regulation of Vps4 ATPase activity by ESCRT-III [PDF]

open access: yesBiochemical Society Transactions, 2009
MVB (multivesicular body) formation occurs when the limiting membrane of an endosome invaginates into the intraluminal space and buds into the lumen, bringing with it a subset of transmembrane cargoes. Exvagination of the endosomal membrane from the cytosol is topologically similar to the budding of retroviral particles and cytokinesis, wherein ...
Brian A, Davies   +2 more
openaire   +2 more sources

Plasma membrane deformation by circular arrays of ESCRT-III protein filaments [PDF]

open access: yes, 2008
Endosomal sorting complex required for transport III (ESCRT-III) proteins function in multivesicular body biogenesis and viral budding. They are recruited from the cytoplasm to the membrane, where they assemble into large complexes.
Hanson, Phyllis I.   +3 more
core   +3 more sources

CC2D1A Is a Regulator of ESCRT-III CHMP4B [PDF]

open access: yesJournal of Molecular Biology, 2012
Endosomal sorting complexes required for transport (ESCRTs) regulate diverse processes ranging from receptor sorting at endosomes to distinct steps in cell division and budding of some enveloped viruses. Common to all processes is the membrane recruitment of ESCRT-III that leads to membrane fission.
Martinelli, Nicolas   +9 more
openaire   +3 more sources

ESCRT-III gets the bends [PDF]

open access: yesJournal of Cell Biology, 2014
![Figure][1] The Vps32 subunits in the ESCRT-III complex naturally assemble into spirals. Shen et al. reveal how a key portion of the membrane-snipping ESCRT-III complex gets in shape.
openaire   +1 more source

ESCRT-III Protein Requirements for HIV-1 Budding [PDF]

open access: yesCell Host & Microbe, 2011
Two early-acting components of the cellular ESCRT pathway, ESCRT-I and ALIX, participate directly in HIV-1 budding. The membrane fission activities of ESCRT-III subunits are also presumably required, but humans express 11 different CHMP/ESCRT-III proteins whose functional contributions are not yet clear.
Morita, Eiji   +5 more
openaire   +2 more sources

Recruitment dynamics of ESCRT-III and Vps4 to endosomes and implications for reverse membrane budding

open access: yeseLife, 2017
The ESCRT machinery mediates reverse membrane scission. By quantitative fluorescence lattice light-sheet microscopy, we have shown that ESCRT-III subunits polymerize rapidly on yeast endosomes, together with the recruitment of at least two Vps4 hexamers.
Manuel Alonso Y Adell   +15 more
doaj   +1 more source

The α-arrestin ARRDC3 mediates ALIX ubiquitination and G protein-coupled receptor lysosomal sorting. [PDF]

open access: yes, 2015
The sorting of G protein-coupled receptors (GPCRs) to lysosomes is critical for proper signaling and cellular responses. We previously showed that the adaptor protein ALIX regulates lysosomal degradation of protease-activated receptor-1 (PAR1), a GPCR ...
Dores, Michael R   +4 more
core   +1 more source

CK2 involvement in ESCRT-III complex phosphorylation

open access: yesArchives of Biochemistry and Biophysics, 2014
The multivesicular body (MVB) sorting pathway is a mechanism for delivering transmembrane proteins into the lumen of the lysosome for degradation. ESCRT-III is the final complex in the pathway that assembles on endosomes and executes membrane scission of intraluminal vesicles.
SALVI, MAURO   +5 more
openaire   +3 more sources

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