Article
Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.
Proceedings of the National Academy of Sciences of the United States of America - 27 Sept 2005
Scott Anna, Gaspar Jason, Stuchell-Brereton Melissa D, Alam Steven L, Skalicky Jack J, Sundquist Wesley I
Abstract excerpt
The VPS4 AAA ATPases function both in endosomal vesicle formation and in the budding of many enveloped RNA viruses, including HIV-1. VPS4 proteins act by binding and catalyzing release of the membrane-associated ESCRT-III protein lattice, thereby allowing multiple rounds of protein sorting and vesicle formation. Here, we report the solution structure of the N-terminal VPS4A microtubule interacting and transport...
Topics
- ATPases Associated with Diverse Cellular Activities
- Adenosine Triphosphatases
- Amino Acid Sequence
- Conserved Sequence
- DNA Mutational Analysis
- Endosomal Sorting Complexes Required for Transport
- Humans
- Leucine
- Membrane Proteins
- Microtubules
- Molecular Sequence Data
- Mutation