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Double C2-like domain-containing protein beta is a protein that in humans is encoded by the DOC2Bgene.[5][6]
Function
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 enhances Ca(2+)-dependent exocytosis in adipocytes,[7]chromaffin cells of the adrenal gland[8] and beta cells in the pancreas.[9] In the central nervous system, Doc2b contributes to the spontaneous release of neurotransmitters , which was thought to be acting as a high-affinity Ca(2+) sensor for exocytosis of synaptic vesicles[10] However, further work has shown that while DOC2b is both important for spontaneous exocytosis of synaptic vesicles and binds Calcium, it does not in fact change the calcium dependence of spontaneous synaptic vesicle release and thus can not be the calcium sensor for this process.[11]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Orita S, Sasaki T, Naito A, Komuro R, Ohtsuka T, Maeda M, Suzuki H, Igarashi H, Takai Y (Feb 1995). "Doc2: a novel brain protein having two repeated C2-like domains". Biochem Biophys Res Commun. 206 (2): 439–48. doi:10.1006/bbrc.1995.1062. PMID7826360.
^Miyazaki M, Emoto M, Fukuda N, Hatanaka M, Taguchi A, Miyamoto S, Tanizawa Y (Jul 2009). "DOC2b is a SNARE regulator of glucose-stimulated delayed insulin secretion". Biochem Biophys Res Commun. 384 (4): 461–5. doi:10.1016/j.bbrc.2009.04.133. PMID19410553.
Duncan RR, Betz A, Shipston MJ, Brose N, Chow RH (1999). "Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo". J. Biol. Chem. 274 (39): 27347–50. doi:10.1074/jbc.274.39.27347. PMID10488064.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Nagano F, Orita S, Sasaki T, Naito A, Sakaguchi G, Maeda M, Watanabe T, Kominami E, Uchiyama Y, Takai Y (1998). "Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport". J. Biol. Chem. 273 (46): 30065–8. doi:10.1074/jbc.273.46.30065. PMID9804756.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Orita S, Naito A, Sakaguchi G, Maeda M, Igarashi H, Sasaki T, Takai Y (1997). "Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery". J. Biol. Chem. 272 (26): 16081–4. doi:10.1074/jbc.272.26.16081. PMID9195900.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Verhage M, de Vries KJ, Røshol H, Burbach JP, Gispen WH, Südhof TC (1997). "DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion". Neuron. 18 (3): 453–61. doi:10.1016/S0896-6273(00)81245-3. PMID9115738.
Kojima T, Fukuda M, Aruga J, Mikoshiba K (1997). "Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta)". J. Biochem. 120 (3): 671–6. doi:10.1093/oxfordjournals.jbchem.a021464. PMID8902635.
Sakaguchi G, Orita S, Maeda M, Igarashi H, Takai Y (1996). "Molecular cloning of an isoform of Doc2 having two C2-like domains". Biochem. Biophys. Res. Commun. 217 (3): 1053–61. doi:10.1006/bbrc.1995.2876. PMID8554557.
Pang ZP, Bacaj T, Yang X, Zhou P, Xu W, Südhof TC (2011). "Doc2 supports spontaneous synaptic transmission by a Ca2+-independent mechanism". Neuron. 70 (2): 244–251. doi:10.1016/j.neuron.2011.03.011. PMID21521611.
