Structural highlights
Function
DCTN1_PIG Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (PubMed:33734450). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).[UniProtKB:Q14203][1]
References
- ↑ Lau CK, O'Reilly FJ, Santhanam B, Lacey SE, Rappsilber J, Carter AP. Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end. EMBO J. 2021 Apr 15;40(8):e106164. PMID:33734450 doi:10.15252/embj.2020106164
