Recombinant Human DYNLL1/PIN protein

Specifications

Form

Liquid

Additional notes

purified by using conventional chromatography techniques

General info

Function

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 (PubMed : 10198631, PubMed : 15193260, PubMed : 15891768, PubMed : 16684779, PubMed : 30464262, PubMed : 37696958). 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 (PubMed : 30464262, PubMed : 37696958). In a subset of DSBs, DYNLL1 remains unphosphorylated and promotes the recruitment of the Shieldin complex (PubMed : 37696958). 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 (PubMed : 15891768, PubMed : 16684779). Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules (PubMed : 10198631, PubMed : 15193260). Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (PubMed : 10198631, PubMed : 15193260).

Sequence similarities

Belongs to the dynein light chain family.

Post-translational modifications

Phosphorylation at Ser-88 promotes recruitment to DNA double-strand breaks (DSBs) by TP53BP1 and ability to inhibit MRE11 (PubMed:37696958). Phosphorylation at Ser-88 appears to control the dimer-monomer transition (PubMed:15193260, PubMed:18650427). According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro (PubMed:15193260, PubMed:18650427).

Subcellular localisation

Cytoskeleton