DYNLL1

Component of dynein, a family of motor proteins essential for movement along microtubules (By similarity). Required for structural and functional integrity of cilia (By similarity). Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). In addition to its role in cytoskeleton and transport, acts as a protein-protein adapter, which inhibits and/or sequesters target proteins. Involved in the response to DNA damage by acting as a key regulator of DNA end resection: when phosphorylated at Ser-88, recruited to DNA double-strand breaks (DSBs) by TP53BP1 and acts by disrupting MRE11 dimerization, thereby inhibiting DNA end resection. In a subset of DSBs, DYNLL1 remains unphosphorylated and promotes the recruitment of the Shieldin complex. Binds and inhibits the catalytic activity of neuronal nitric oxide synthase/NOS1 (By similarity). Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity..

Function from UniProtKB (P63167), read 2026-09-23. CC BY 4.0.