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An expanded list of LC8 binding partners revealed the evolutionary plasticity of binding partners despite the highly conserved binding interface. In addition, it also highlighted a novel, conserved function of LC8 in the upstream regulation of the Hippo signaling pathway.
DLC1 binding to nNOS-calmodulin complex does not affect the electron transport from the reductase to the oxygenase domain.
NMR-derived secondary chemical shifts and relaxation properties show that the Chica (show FAM83D Proteins) LC8 binding domain is essentially disordered with a dynamically restricted segment in one linker between motifs.
Studies indicate that dynein light chain LC8 has been termed an intrinsically disordered proteins (IDPs) dimerization 'hub' protein.
DLC1 binding motif in L is involved in cytoskeleton localization and reorganization, primary transcription regulation by DLC1, and regulation of cellular DLC1 gene expression.
The dynein light intermediate chain has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins.
Authors demonstrate that the interaction between ebola virus VP35 and dynein LC8 is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis.
Overall, this study demonstrates the novel interaction between HIV-1 integrase and cellular DYNLL1 proteins and suggests the requirement of this virus-cell interaction for proper uncoating and efficient reverse transcription of HIV-1.
Structural analysis of LC8 with both Nek9 (show NEK9 Proteins) peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 (show NEK9 Proteins) to LC8 upon phosphorylation on Ser (show SIGLEC1 Proteins)(944) within the Nek9 (show NEK9 Proteins) sequence
Dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis.
oncogenic MYC (show MYC Proteins) expression, which is synthetic lethal with Dynll1 deletion in B-2 cells, did not further reduce B-1a cell numbers in Dynll1-defcient mice. we found that the ASCIZ (show ATMIN Proteins)-DYNLL1 axis was also required for the early-juvenile development of aggressive MYC (show MYC Proteins)-driven and p53 (show TP53 Proteins)-deficient B cell lymphomas.
ASCIZ (show ATMIN Proteins) and its target DYNLL1 are essential for the development and expansion of MYC (show MYC Proteins)-driven B cell lymphoma.
These findings uncovered the surprising functional relevance of GTP-bound Arl3 and LC8 for the unloading regulation of dynactin-bound cargo from dynein motor.
a key role for ASCIZ (show ATMIN Proteins) in regulating the survival of developing B cells by activating DYNLL1 expression, which may then modulate Bim (show BCL2L11 Proteins)-dependent apoptosis
The ASCIZ (show ATMIN Proteins)-DYNLL1 feedback loop represents a novel mechanism for auto-regulation of gene expression, where the gene product directly inhibits the transcriptional activator while bound at its own promoter.
the regulation of DLC1 by p21-activated kinase 1 (show PAK1 Proteins) is a novel mechanism by which a signaling kinase might influence macropinocytosis
PIN/LC8 is associated with cytosolic but not membrane-bound nNOS (show NOS1 Proteins) in the nitrergic varicosities of mice gut (show GUSB Proteins).
Our studies suggest an unexpected role for LC8 and provide new mechanistic insights into how SNPH (show SNPH Proteins) and LC8 together immobilize mitochondria through a dynamic interaction between the docking receptor and axonal cytoskeleton.
LC8 promotes assembly and stabilization of microtubules.
By yeast two-hybrid assay, the authors found that the capsid protein (CA) of bovine immunodeficiency virus interacted with the dynein light-chain component LC8.
DYNLL1, mediated porcine circovirus type 2 intracellular trafficking.
Large dynein heads take 16-nm steps by using an overlapping hand-over-hand mechanism.
DLC-1 directly binds to FBF-2 outside of the RNA-binding domain and promotes FBF-2 localization and function. This result identifies a new role for DLC-1 in post-transcriptional regulation of gene expression.
DLC-1 is functioning cell nonautonomously through the same pathway as kri-1 (show KRI1 Proteins) in response to ionizing radiation-induced apoptosis.
Dynein light chain 1 (DLC-1) and its partner, dynein heavy chain 1, inhibit the proliferative cell fate, in part through regulation of METT-10, a conserved putative methyltransferase.
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.
8 kDa dynein light chain
, cytoplasmic dynein light polypeptide
, dynein light chain 1, cytoplasmic
, dynein, cytoplasmic, light polypeptide 1
, protein inhibitor of neuronal nitric oxide synthase
, dynein light chain 2
, dynein, light chain, LC8-type 2
, 8kD LC
, 8kDa LC
, dynein, cytoplasmic, light chain 1
, dynein, cytoplasmic, light peptide
, protein inhibitor of nitric oxide synthase
, dynein LC8
, dynein, light chain, LC8-type 1
, dynein, light chain, LC8-type 1a
, dynein light chain LC8-type 1
, dynein, light chain, LC8-type 1b
, cytoplasmic light-chain dynein