Biology:DOC2B
 Generic protein structure example |
Double C2-like domain-containing protein beta is a protein that in humans is encoded by the DOC2B gene.[1][2]
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,[3] chromaffin cells of the adrenal gland[4] and beta cells in the pancreas.[5] 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 [6] 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.[7]
References
- ↑ "Doc2: a novel brain protein having two repeated C2-like domains". Biochem Biophys Res Commun 206 (2): 439–48. Feb 1995. doi:10.1006/bbrc.1995.1062. PMID 7826360.
- ↑ "Entrez Gene: DOC2B double C2-like domains, beta". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8447.
- ↑ "DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes". Diabetes 58 (2): 377–84. Feb 2009. doi:10.2337/db08-0303. PMID 19033398.
- ↑ "DOC2B acts as a calcium switch and enhances vesicle fusion". J Neurosci 28 (27): 6794–806. Jul 2008. doi:10.1523/JNEUROSCI.0538-08.2008. PMID 18596155.
- ↑ "DOC2b is a SNARE regulator of glucose-stimulated delayed insulin secretion". Biochem Biophys Res Commun 384 (4): 461–5. Jul 2009. doi:10.1016/j.bbrc.2009.04.133. PMID 19410553.
- ↑ "Doc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter release". Science 327 (5973): 1614–8. Mar 2010. doi:10.1126/science.1183765. PMID 20150444.
- ↑ *"Doc2 supports spontaneous synaptic transmission by a Ca2+-independent mechanism". Neuron 70 (2): 244–251. 2011. doi:10.1016/j.neuron.2011.03.011. PMID 21521611.
Further reading
- "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". Am. J. Hum. Genet. 72 (4): 918–30. 2003. doi:10.1086/374320. PMID 12621583.
- "Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo". J. Biol. Chem. 274 (39): 27347–50. 1999. doi:10.1074/jbc.274.39.27347. PMID 10488064.
- "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. 1998. doi:10.1074/jbc.273.46.30065. PMID 9804756.
- "Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery". J. Biol. Chem. 272 (26): 16081–4. 1997. doi:10.1074/jbc.272.26.16081. PMID 9195900.
- "DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion". Neuron 18 (3): 453–61. 1997. doi:10.1016/S0896-6273(00)81245-3. PMID 9115738.
- "Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta)". J. Biochem. 120 (3): 671–6. 1997. doi:10.1093/oxfordjournals.jbchem.a021464. PMID 8902635.
- "Molecular cloning of an isoform of Doc2 having two C2-like domains". Biochem. Biophys. Res. Commun. 217 (3): 1053–61. 1996. doi:10.1006/bbrc.1995.2876. PMID 8554557.
- "Doc2 supports spontaneous synaptic transmission by a Ca2+-independent mechanism". Neuron 70 (2): 244–251. 2011. doi:10.1016/j.neuron.2011.03.011. PMID 21521611.
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