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Human Polyclonal DOC2B Primary Antibody for WB - ABIN521906
Yao, Gaffaney, Kwon, Chapman: Doc2 is a Ca2+ sensor required for asynchronous neurotransmitter release. in Cell 2011
Reduction of DOC2B is an early feature of T1 diabetes (T1D), and DOC2B abundance may serve as a valuable in vivo indicator of beta-cell mass and an early biomarker of T1D.
Here the authors report that analogous ring-like oligomers assemble from the C2AB domains of other Syt isoforms (Syt2, Syt7, Syt9) as well as related C2 domain containing protein, Doc2B and extended Synaptotagmins (E-Syts).
promoter hypermethylation and silencing of the DOC2B gene is an early and frequent event during cervical carcinogenesis and whose reduced expression due to DNA promoter methylation may lead to selective cervical tumor growth
Study analyzed Doc2alpha and Doc2beta and found that Doc2 responds to changes in [Ca2+], with markedly slower kinetics as compared to the cytosolic domain of syt I (syt), and operates on a timescale consistent with asynchronous neurotransmitter release.
Doc2b enrichment in the beta-cell protects against diabetogenic and proapoptotic stress.
Mutating Ca(2+)-coordinating aspartates in the C2A-domain localizes Doc2B permanently at the plasma membrane, and renders an upstream priming step Ca(2+)-independent, whereas a separate function in downstream priming depends on SNARE-binding, Ca(2+)-binding to the C2B-domain of Doc2B, interaction with ubMunc13-2 and the presence of synaptotagmin-1.
study identifies a critical role for DOC2B in insulin-stimulated glucose uptake in adipocytes, and for the synergistic regulation of GSIS by DOC2A and DOC2B in beta cells.
Data demonstrate that Munc13-1 and DOC2B have different effects on network activity and that by enhancing asynchronous release, DOC2B exerts its properties to increase spiking activity and elevate synchronization between neurons within network bursts
Hence these data support a working model wherein Doc2b functions as a docking platform/scaffold for transient interactions with the multiple Munc18 isoforms operative in insulin release, promoting SNARE assembly.
Doc2b is a limiting factor in SNARE exocytosis events pertinent to glycaemic regulation in vivo. Doc2b enrichment may provide a novel means to simultaneously boost islet and skeletal muscle function in vivo in the treatment and/or prevention of diabetes.
Mutations that disrupt Ca(2)-binding activity endow Doc2beta with novel functional properties during synaptic transmission.
Doc2b acts to inhibit vesicle priming during prolonged calcium elevations, thus protecting unprimed vesicles from fusing prematurely, and redirecting them to refill the readily releasable pool after relaxation of the calcium signal.
Doc2b is a key positive regulator of Munc18c-syntaxin 4-mediated insulin secretion as well as of insulin responsiveness in skeletal muscle, and thus a key effector for glucose homeostasis in vivo.
The data of this study suggested that Doc2s are modulators of spontaneous synaptic transmission that act by a Ca(2+)-independent mechanism.
study found that Doc2b is a high-affinity Ca2+ sensor for half (hippocampus) or most (cerebellum) of the spontaneous neurotransmitter release events in CNS synapses
tyrosine phosphorylation of Munc18c induces a switch in binding specificity from syntaxin 4 to Doc2beta
We conclude that DOC2B is a calcium-dependent priming factor and its activity at the PM enables efficient expansion of the fusion pore, leading to increased catecholamine release.
Fndings indicate that DOC2b is a positive SNARE regulator for GLUT4 vesicle fusion and mediates insulin-stimulated glucose transport in adipocytes.
These data suggest that DOC2b may be a regulator for delayed (second-phase) insulin secretion in MIN6 cells.
There are at least two protein isoforms of the Double C2 protein, namely alpha (DOC2A) and beta (DOC2B), which contain two C2-like domains. DOC2A and DOC2B are encoded by different genes\; these genes are at times confused with the unrelated DAB2 gene which was initially named DOC-2. DOC2B is expressed ubiquitously and is suggested to be involved in Ca(2+)-dependent intracellular vesicle trafficking in various types of cells.
double C2-like domains, beta-like
, double C2-like domains, beta
, double C2-like domain-containing protein beta-like
, double C2, beta
, double C2-like domain-containing protein beta
, double C2 protein beta