DYNLL1

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. [provided by RefSeq]

dynein, light chain, LC8-type 1

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. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.

Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.

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.

Apoptotic process Source: UniProtKB-KW
Cilium assembly Source: GO_Central
Microtubule-based process Source: InterPro
Negative regulation of nitric oxide biosynthetic process Source: Ensembl
Negative regulation of phosphorylation Source: UniProtKB
Positive regulation of ATP-dependent microtubule motor activity, plus-end-directed Source: GO_Central
Positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
Spermatid development Source: Ensembl
Substantia nigra development Source: UniProtKB

Mitochondrion; Centrosome; Cytoskeleton; Nucleus. Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.

Phosphorylation at Ser-88 appears to control the dimer-monomer transition. 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.