(Q35861018)

English

Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).

scientific article published in April 2015

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scholarly article

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Europe PubMed Central

PMC publication ID

10 August 2017

Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs). (English)

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

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author name string

Han Han

1

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Nicole Monroe

2

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Jörg Votteler

3

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Binita Shakya

4

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Wesley I Sundquist

5

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Christopher P Hill

6

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Europe PubMed Central

PMC publication ID

10 August 2017

language of work or name

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publication date

1 April 2015

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Europe PubMed Central

PMC publication ID

10 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

PMC publication ID

10 August 2017

290

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

21

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

13490-13499

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Mechanistic insights into the recycling machine of the SNARE complex

1 reference

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Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4.

1 reference

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Vfa1 Binds to the N-terminal Microtubule-interacting and Trafficking (MIT) Domain of Vps4 and Stimulates Its ATPase Activity

1 reference

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Nucleotide-induced asymmetry within ATPase activator ring drives 54-RNAP interaction and ATP hydrolysis

1 reference

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The Oligomeric State of the Active Vps4 AAA ATPase

1 reference

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The linker region plays a regulatory role in assembly and activity of the Vps4 AAA ATPase

1 reference

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Membrane fission reactions of the mammalian ESCRT pathway

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Design principles of a universal protein degradation machine

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Structure and function of the membrane deformation AAA ATPase Vps4.

1 reference

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Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments

1 reference

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Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition

1 reference

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11 July 2018

Structural Role of the Vps4-Vta1 Interface in ESCRT-III Recycling

1 reference

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Membrane budding and scission by the ESCRT machinery: it's all in the neck

1 reference

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11 July 2018

Assembly of the AAA ATPase Vps4 on ESCRT-III.

1 reference

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The cell biology of HIV-1 virion genesis

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Structural basis for ESCRT-III protein autoinhibition

1 reference

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Three-dimensional structure of AAA ATPase Vps4: advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding

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Biochemical and Structural Studies of Yeast Vps4 Oligomerization

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Helical structures of ESCRT-III are disassembled by VPS4

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Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding

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Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly

1 reference

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Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p

1 reference

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Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p

1 reference

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1 reference

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1 reference

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1 reference

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ESCRT-III recognition by VPS4 ATPases

1 reference

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1 reference

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Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis

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Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing

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Evolutionary relationships and structural mechanisms of AAA+ proteins

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

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1 reference

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Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.

1 reference

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AAA+ proteins: have engine, will work

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The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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ESCRT machinery is required for plasma membrane repair.

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ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1.

1 reference

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Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel

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Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component

1 reference

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12 December 2020

based on heuristic

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Identifiers

10.1074/JBC.M115.642355

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

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