Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry

Biochemical and Biophysical Research Communications
Shin-ichi TerawakiKaori Wakamatsu

Abstract

Bicaudal-D1 (BICD1) is an α-helical coiled-coil protein mediating the attachment of specific cargo to cytoplasmic dynein. It plays an essential role in minus end-directed intracellular transport along microtubules. The third C-terminal coiled-coil region of BICD1 (BICD1 CC3) has an important role in cargo sorting, including intracellular vesicles associating with the small GTPase Rab6 and the nuclear pore complex Ran binding protein 2 (RanBP2), and inhibiting the association with cytoplasmic dynein by binding to the first N-terminal coiled-coil region (CC1). The crystal structure of BICD1 CC3 revealed a parallel homodimeric coiled-coil with asymmetry and complementary knobs-into-holes interactions, differing from Drosophila BicD CC3. Furthermore, our binding study indicated that BICD1 CC3 possesses a binding surface for two distinct cargos, Rab6 and RanBP2, and that the CC1-binding site overlaps with the Rab6-binding site. These findings suggest a molecular basis for cargo recognition and autoinhibition of BICD proteins during dynein-dependent intracellular retrograde transport.

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Citations

Jan 30, 2016·Trends in Cell Biology·Casper C Hoogenraad, Anna Akhmanova
May 18, 2016·Biotechnology and Bioengineering·Anett RitterHolger Laux
Jul 19, 2017·ELife·William B RedwineSamara L Reck-Peterson
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Jun 27, 2018·ELife·Thomas E SladewskiKathleen M Trybus
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Nov 23, 2018·Cell Death and Differentiation·Hyun Jik LeeHo Jae Han
Mar 17, 2019·Journal of Cell Science·Mara A Olenick, Erika L F Holzbaur
Jul 2, 2016·The Journal of Biological Chemistry·Mara A OlenickErika L F Holzbaur
Feb 23, 2020·Journal of Cell Science·Marta I BudzinskaGiampietro Schiavo
Mar 19, 2021·The EMBO Journal·Clinton K LauAndrew P Carter
Oct 23, 2018·Biochemistry·Crystal R NoellSozanne R Solmaz
Jul 16, 2019·The Journal of Physical Chemistry Letters·Crystal R NoellSozanne R Solmaz

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