Human cytoplasmic dynein bound to Lis1
Ontology highlight
ABSTRACT:
SUBMITTER: Andres Leschziner
PROVIDER: EMPIAR-11373 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structures of human dynein in complex with the lissencephaly 1 protein, LIS1.
Reimer Janice M JM DeSantis Morgan E ME Reck-Peterson Samara L SL Leschziner Andres E AE
eLife 20230124
The lissencephaly 1 protein, LIS1, is mutated in type-1 lissencephaly and is a key regulator of cytoplasmic dynein-1. At a molecular level, current models propose that LIS1 activates dynein by relieving its autoinhibited form. Previously we reported a 3.1 Å structure of yeast dynein bound to Pac1, the yeast homologue of LIS1, which revealed the details of their interactions (Gillies et al., 2022). Based on this structure, we made mutations that disrupted these interactions and showed that they w ...[more]
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