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this study, members of the Doc2 family (show RPH3A Proteins) of presynaptic proteins were eliminated, which caused a reduction in spontaneous neurotransmission, whereas action potential-evoked neurotransmission remained relatively normal.
Study analyzed Doc2alpha and Doc2beta and found that Doc2 (show DAB2 Proteins) responds to changes in [Ca2 (show CA2 Proteins)+], with markedly slower kinetics as compared to the cytosolic domain of syt I (syt (show SYT1 Proteins)), and operates on a timescale consistent with asynchronous neurotransmitter release.
study identifies a critical role for DOC2B (show DOC2B Proteins) in insulin (show INS Proteins)-stimulated glucose uptake in adipocytes, and for the synergistic regulation of GSIS by DOC2A and DOC2B (show DOC2B Proteins) in beta cells.
The polybasic sequence in the C2B domain functions as a binding site for syntaxin-1a (show STX1A Proteins)/SNAP-25 (show SNAP25 Proteins) heterodimer and controls the number of 'readily releasable' vesicles in neuroendocrine 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. DOC2A is mainly expressed in brain and is suggested to be involved in Ca(2+)-dependent neurotransmitter release.
double C2-like domains, alpha
, secretory vesicle-associated protein DOC2
, double C2-like domain-containing protein alpha
, double C2, alpha