Dynein Light Chain 1, Cytoplasmic Protein (DYNLL1) Recombinant Protein

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, Jul 2008]

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. 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. Ref.3 Ref.5 Ref.7 Ref.9Binds and inhibits the catalytic activity of neuronal nitric oxide synthase. Ref.3 Ref.5 Ref.7 Ref.9Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. Ref.3 Ref.5 Ref.7 Ref.9Regulates 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. Ref.3 Ref.5 Ref.7 Ref.9

Subunit structure: Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. 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. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with rabies P protein

By similarity. Interacts with TXNDC17. Interacts with WWC1 and ESR1. The WWC1-DYNLL1 interaction is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11 isoform 1 and isoform 2. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1. Interacts with human spumaretrovirus Gag protein; this interaction is critical for intracellular microtubule-dependent viral genome transport toward the centrosome. Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing SKAP, SPAG5, PLK1, DYNLL1 and SGOL2. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.14

Subcellular location: Cytoplasm › cytoskeleton. Nucleus. Mitochondrion. Note: Upon induction of apoptosis translocates together with BCL2L11 to mitochondria. Ref.1 Ref.7

Tissue specificity: Ubiquitous. Ref.1

Induction: Up-regulated by PAK1 and estrogen. Ref.3 Ref.5 Ref.7

Post-translational modification: Phosphorylation at Ser-88 appears to control the dimer-monomer transition. According to Ref.5, it is phosphorylated at Ser-88 by PAK1, however, according to Ref.11, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro. Ref.5 Ref.12

Sequence similarities: Belongs to the dynein light chain family.