Recombinant Human Dynein light chain 1, Cytoplasmic domain (DYNLL1)

Function

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 (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)

Subcellular Location

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Chromosome; Cytoplasm, cytoskeleton; Nucleus; Mitochondrion

Tissue Specificity

Ubiquitous (PubMed:8628263). Expressed in testis (PubMed:22965910)

Subunit

(Microbial infection) Interacts with ebolavirus protein VP35; this interaction stabilizes VP35 N-terminal oligomerization domain and enhances viral RNA synthesis

• Dick T. et al. Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. — Mol. Cell. Biol. (1996)
• Ebert L. et al. Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). (MAY-)
• Puthalakath H. et al. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. — Mol. Cell (1999)
• Petit C. et al. Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8. — J. Cell Sci. (2003)
• Andersen J.S. et al. Proteomic characterization of the human centrosome by protein correlation profiling. — Nature (2003)
• Vadlamudi R.K. et al. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. — Cancer Cell (2004)
• Jeong W. et al. Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways. — J. Biol. Chem. (2004)
• Rayala S.K. et al. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. — EMBO Rep. (2005)