A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity

In-Gyun Lee, Mara A. Olenick, Malgorzata Boczkowska, Clara Franzini-Armstrong, Erika L. F. Holzbaur and Roberto Dominguez ()
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In-Gyun Lee: University of Pennsylvania
Mara A. Olenick: University of Pennsylvania
Malgorzata Boczkowska: University of Pennsylvania
Clara Franzini-Armstrong: University of Pennsylvania
Erika L. F. Holzbaur: University of Pennsylvania
Roberto Dominguez: University of Pennsylvania

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract Cytoplasmic dynein is the major minus-end-directed microtubule-based motor in cells. Dynein processivity and cargo selectivity depend on cargo-specific effectors that, while generally unrelated, share the ability to interact with dynein and dynactin to form processive dynein–dynactin-effector complexes. How this is achieved is poorly understood. Here, we identify a conserved region of the dynein Light Intermediate Chain 1 (LIC1) that mediates interactions with unrelated dynein–dynactin effectors. Quantitative binding studies map these interactions to a conserved helix within LIC1 and to N-terminal fragments of Hook1, Hook3, BICD2, and Spindly. A structure of the LIC1 helix bound to the N-terminal Hook domain reveals a conformational change that creates a hydrophobic cleft for binding of the LIC1 helix. The LIC1 helix competitively inhibits processive dynein–dynactin-effector motility in vitro, whereas structure-inspired mutations in this helix impair lysosomal positioning in cells. The results reveal a conserved mechanism of effector interaction with dynein–dynactin necessary for processive motility.

Date: 2018
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DOI: 10.1038/s41467-018-03412-8

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