Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae.
Subcellular localization of the yeast proteome.
The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast.
NudEL targets dynein to microtubule ends through LIS1.
High-quality binary protein interaction map of the yeast interactome network.
Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor.
The social and structural architecture of the yeast protein interactome.
LIS1 at the microtubule plus end and its role in dynein-mediated nuclear migration.
Structural basis for cytoplasmic dynein-1 regulation by Lis1.
Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.
The dynein cortical anchor Num1 activates dynein motility by relieving Pac1/LIS1-mediated inhibition.
Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex.
A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.
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Purified yeast Pac1 binds dynein with nucleotide-state-dependent stoichiometry, and the 1 dynein:1 Pac1 dimer state helps open or stabilize an uninhibited dynein conformation through linker contacts required for dynein-mediated spindle movement in cells.
"Our results support a model in which Lis1 can indeed open and/or stabilize an uninhibited conformation of dynein but only when the AAA domains are in specific nucleotide-bound states."