Structural Basis of Ist1 Function and Ist1–Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis
Copyright policy )Structural Basis of Ist1 Function and Ist1–Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis
The ESCRT machinery functions in several important eukaryotic cellular processes. The AAA-ATPase Vps4 catalyzes disassembly of the ESCRT-III complex and may regulate membrane deformation and vesicle scission as well. Ist1 was proposed to be a regulator of Vps4, but its mechanism of action was unclear. The crystal structure of the N-terminal domain of Ist1 (Ist1NTD) reveals an ESCRT-III subunit-like fold, implicating Ist1 as a divergent ESCRT-III family member. Ist1NTD specifically binds to the ESCRT-III subunit Did2, and cocrystallization of Ist1NTD with a Did2 fragment shows that Ist1 interacts with the Did2 C-terminal MIM1 (MIT-interacting motif 1) via a novel MIM-binding structural motif. This arrangement indicates a mechanism for intermolecular ESCRT-III subunit association and may also suggest one form of ESCRT-III subunit autoinhibition via intramolecular interaction.
- University of Michigan–Flint United States
- Life Sciences Institute United States
- Mayo Clinic United States
- University of Michigan–Ann Arbor United States
Models, Molecular, Binding Sites, Microscopy, Confocal, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Sequence Homology, Amino Acid, Molecular Sequence Data, Multivesicular Bodies, Vesicular Transport Proteins, Membrane Proteins, Surface Plasmon Resonance, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Microscopy, Fluorescence, Amino Acid Sequence, Cytokinesis, Protein Binding
Models, Molecular, Binding Sites, Microscopy, Confocal, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Sequence Homology, Amino Acid, Molecular Sequence Data, Multivesicular Bodies, Vesicular Transport Proteins, Membrane Proteins, Surface Plasmon Resonance, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Microscopy, Fluorescence, Amino Acid Sequence, Cytokinesis, Protein Binding
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).84 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!