Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility.

ABSTRACT: Cytoplasmic dynein is the primary minus-end-directed microtubule motor protein in animal cells, performing a wide range of motile activities, including transport of vesicular cargos, mRNAs, viruses, and proteins. Lissencephaly-1 (LIS1) is a highly conserved dynein-regulatory factor that binds directly to the dynein motor domain, uncoupling the enzymatic and mechanical cycles of the motor and stalling dynein on the microtubule track. Dynactin, another ubiquitous dynein-regulatory factor, releases dynein from an autoinhibited state, leading to a dramatic increase in fast, processive dynein motility. How these opposing activities are integrated to control dynein motility is unknown. Here, we used fluorescence single-molecule microscopy to study the interaction of LIS1 with the processive dyne

SUBMITTER: Gutierrez PA 

PROVIDER: S-EPMC5519373 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature