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Human Polyclonal KLC1 Primary Antibody pour FACS, IHC (p) - ABIN652577
Chernajovsky, Brown, Clark: Human kinesin light (beta) chain gene: DNA sequence and functional characterization of its promoter and first exon. dans DNA and cell biology 1997
Show all 2 Pubmed References
extensive biochemical characterization of the KLC:JIP1 interaction, as well as identification of potential KLC1-binding partners, improves the understanding of how this growing family of cargos is recruited to kinesin1 by KLC1.
structural plasticity of the N-terminal capping helix might represent a structural determinant for TPR domain structural versatility in cargo binding
All binary complexes (KLC1:APP, KLC1:JIP1, and APP:JIP1) contain conformations with favorable binding free energies indicating that KLC1 and JIP1 may take part in APP transport in Alzheimer's disease patients.
BNIP-2 is a kinesin-1 adapter involved in vesicular transportation in the cytoplasm and that association with cargos depends on interaction of the CRAL-TRIO domain with membrane phosphatidylserine.
The G allele and GG genotype of KLC1 rs8702 were significantly over-represented among cataract patients, as compared to healthy controls, and were associated with an odds ratio for cataract development.
Dnm1L interacts with KLC1 through the tetratricopeptide repeat domains.
Microtubule-bound kinesin-1 and kinesin-3 motor domains were visualized at multiple steps in their ATPase cycles--including their nucleotide-free states--at approximately 7 A resolution using cryo-electron microscopy.
Studies indicate that FEZ1 (fasciculation and elongation protein zeta 1), SCOCO (short coiled-coil protein) and kinesins (kinesin heavy chain) are involved in biological transport process.
The expression levels of KLC1 variant E in brain and lymphocytes were significantly higher in Alzheimer's disease patients.
study provides evidence that the combined effect of three variants within the KLC1 gene may predispose to age-related cataract.
For the binding of cargos shared by KLC1, we propose a different site located within the groove but not involving N343.
Data suggest that KLC1 is required for normal neural differentiation, ensuring proper metabolism of AD-associated molecules APP and Tau and for proliferation of neural precursors (NPs).
Phosphorylation of KLC1 at serine 460 modulates binding and trafficking of calsyntenin-1.
Results do not convincingly support kinesin light chain 1 (KLC1) as a major susceptibility gene in any of the studied diseases, although there is a small effect of KLC1 in relation to cataract.
The major binding site for kinesin light chain in kinesin heavy chain has been mapped to residues 789-813 at the C-terminal end of the heavy chain stalk domain.
For a single nucleotide polymorphism (G58836C in intron 13) in the kinesin light-chain 1 (KNS2) gene, the association between Alzheimer's disease and the C allele is found to be significant.
KNS2 gene may play a role during early stages of Alzheimer's disease pathogenesis.
KLC1 gene may be a novel susceptibility gene for age-related cataract.
microtubule-dependent functions of von Hippel-Lindau tumour suppressor are influenced by kinesin-2
The present finding supports the involvement of the cytoskeleton and KNS2 in the development of vascular white matter damage, thereby opening up novel fields in the research into leukariois.
kinesin-1 recognizes a novel class of adaptor motifs 'Y-acidic' (tyrosine flanked by acidic residues), in a KLC-isoform-specific manner.
KLC1 deletion leads to a reduction of Mn2+ transport from CA3 to the septal nuclei.
Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 binding to kinesin-1 decreased, suggesting that APP transport is impaired by aging. Authors conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP by kinesin-1 by modulating its interaction with JIP1b.
In old mice, lack of KLC1 results in retinal pigment epithelium pathogenesis that was strikingly comparable to aspects of age-related macular degeneration.
Alcalpha is efficiently processed in part to minimize the inappropriate peripheral retention of kinesin-1
A small peptide sequence is sufficient for initiating kinesin-1 activation through part of TPR region of KLC1
Data show that amyloid precursor protein (APP) levels are well-correlated with the amount of the light chain of kinesin-1 (KLC1).
KLC1-ALK is the first novel oncogenic fusion identified using only formalin-fixed paraffin-embedded tissue tissues
changes in the phosphorylation state of KLC1 at Ser517/520 are unlikely to affect motor function.
An essential role of mNUDC for anterograde transport of dynein and dynactin by kinesin-1.
Impairment of anterograde transport by knockdown of KIF5B or KLC1 delayed stress-granule dissolution.
analysis of a novel protein-protein interaction between KLC1 and JLP that involves leucine zipper-like domains
Calsyntenin-1 links a certain type of vesicular and tubulovesicular organelles to the Kinesin-1 motor.
Both oAbeta and CK2 treatment of axoplasm led to increased phosphorylation of kinesin-1 light chains and subsequent release of kinesin from its cargoes
KLC1, a molecule involved in dendritic and axonal transport in the brain, is affected during chronic morphine treatment and may be involved in the development of opioid addiction.
Conventional kinesin is a tetrameric molecule composed of two heavy chains and two light chains, and transports various cargos along microtubules toward their plus ends. The heavy chains provide the motor activity, while the light chains bind to various cargos. This gene encodes a member of the kinesin light chain family. It associates with kinesin heavy chain through an N-terminal domain, and six tetratricopeptide repeat (TPR) motifs are thought to be involved in binding of cargos such as vesicles, mitochondria, and the Golgi complex. Thus, kinesin light chains function as adapter molecules and not motors per se. Although previously named 'kinesin 2', this gene is not a member of the kinesin-2 / kinesin heavy chain subfamily of kinesin motor proteins. Extensive alternative splicing produces isoforms with different C-termini that are proposed to bind to different cargos\; however, the full-length nature and/or biological validity of most of these variants have not been determined.
, kinesin light chain 1
, kinesin light chain 2
, kinesin light chain 4
, kinesin 2 60/70kDa
, kinesin ii
, KLC 1
, medulloblastoma antigen MU-MB-2.50