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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).SUBUNIT Homodimer (PubMed:18084006, PubMed:18650427). Monomer; the monomeric form is incapable of binding to target proteins (PubMed:18084006, PubMed:18650427). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition (By similarity). The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits (By similarity). The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer (By similarity). Part of the ciliary outer dynein arms (ODAs), at least consisting of dynein axonemal heavy chains, light chains and intermediate chains (By similarity). The ODAs interact with DNAAF9; this interaction inactivates the dyneins (By similarity). Interacts with TXNDC17 (PubMed:14607843). Interacts with WWC1 and ESR1 (PubMed:15891768, PubMed:16684779, PubMed:24682284). The WWC1-DYNLL1 interaction is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin (PubMed:15891768, PubMed:16684779). Interacts with BCL2L11 isoform 1 and isoform 2 (PubMed:10198631, PubMed:15193260). Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis (PubMed:10198631). Interacts with PAK1; the interaction requires dimeric DYNLL1 (PubMed:15193260, PubMed:18650427). Interacts with MYZAP (PubMed:20412299). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (PubMed:21402792). Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN (PubMed:22167198). Interacts with NEK9 (not phosphorylated at 'Ser-944') (PubMed:23482567). Interacts with BICD2 (By similarity). Interacts with BCAS1 (By similarity). Interacts with Basson/BSN (PubMed:19380881). Interacts with HDAC6 (PubMed:31505170). Interacts with TPPP (PubMed:31505170). Interacts with AMBRA1 (via TQT motifs); tethering AMBRA1 to the cytoskeleton (PubMed:20921139). Interacts with FAM83D/CHICA (via C-terminus) (PubMed:22965910). Interacts with HMMR, SPAG5/Astrin and KNSTRN/Kinastrin (PubMed:22965910). Interacts with TLK2 (PubMed:29955062, PubMed:33323470). Interacts with NOS1 (By similarity). Interacts with WWC1, WWC2 and WWC3 (PubMed:24682284). Interacts with MRE11; inhibiting MRE11 homodimerization and activity (PubMed:30464262, PubMed:37696958).SUBUNIT (Microbial infection) Interacts with human spumaretrovirus Gag protein; this interaction is critical for intracellular microtubule-dependent viral genome transport toward the centrosome.SUBUNIT (Microbial infection) Interacts with ebolavirus protein VP35; this interaction stabilizes VP35 N-terminal oligomerization domain and enhances viral RNA synthesis.INTERACTION Upon induction of apoptosis translocates together with BCL2L11 to mitochondria (PubMed:18084006). Recruited to DNA double-strand breaks (DSBs) by TP53BP1 when phosphorylated at Ser-88 (PubMed:37696958).TISSUE SPECIFICITY Ubiquitous (PubMed:8628263). Expressed in testis (PubMed:22965910).INDUCTION Up-regulated by ATMIN, PAK1 and estrogen.PTM 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).SIMILARITY Belongs to the dynein light chain family.
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