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

Lee, In-Gyun ; Olenick, Mara A ; Boczkowska, Malgorzata ; Franzini-Armstrong, Clara ; Holzbaur, Erika L F ; Dominguez, Roberto

Nature communications, 2018-03, Vol.9 (1), p.986-12, Article 986 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity
Autor: Lee, In-Gyun ; Olenick, Mara A ; Boczkowska, Malgorzata ; Franzini-Armstrong, Clara ; Holzbaur, Erika L F ; Dominguez, Roberto
Assuntos: Amino Acid Sequence ; Binding ; Chains ; Cytoplasmic Dyneins - chemistry ; Cytoplasmic Dyneins - metabolism ; Dynactin ; Dynactin Complex - metabolism ; Dynein ; Effectors ; HeLa Cells ; Humans ; Hydrophobicity ; Motility ; Movement ; Mutation ; Positioning devices (machinery) ; Protein Conformation
É parte de: Nature communications, 2018-03, Vol.9 (1), p.986-12, Article 986
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: 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.
Editor: England: Nature Publishing Group
Idioma: Inglês

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

Lee, In-Gyun ; Olenick, Mara A ; Boczkowska, Malgorzata ; Franzini-Armstrong, Clara ; Holzbaur, Erika L F ; Dominguez, Roberto

England: Nature Publishing Group

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