# DOC2B

> Mediated Wiki article. Canonical URL: https://mediated.wiki/source/DOC2B
> Markdown URL: https://mediated.wiki/source/DOC2B.md
> Source: https://en.wikipedia.org/wiki/DOC2B
> Source revision: 1350641774
> License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/)

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Double C2-like domain-containing protein beta''' is a [protein](/source/protein) that in humans is encoded by the ''DOC2B'' [gene](/source/gene).<ref name="pmid7826360">{{cite journal | vauthors = Orita S, Sasaki T, Naito A, Komuro R, Ohtsuka T, Maeda M, Suzuki H, Igarashi H, Takai Y | title = Doc2: a novel brain protein having two repeated C2-like domains | journal = Biochem Biophys Res Commun | volume = 206 | issue = 2 | pages = 439–48 | date = Feb 1995 | pmid = 7826360 | doi = 10.1006/bbrc.1995.1062 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DOC2B double C2-like domains, beta| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8447| access-date = }}</ref>

== Function ==

There are at least two protein [isoforms](/source/protein_isoform) of the Double C2 protein,  namely alpha ([DOC2A](/source/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. In mouse and rat tissue, Doc2b enhances Ca<sup>2+</sup>-dependent [exocytosis](/source/exocytosis) in [adipocytes](/source/adipocytes),<ref name="pmid19033398">{{cite journal | vauthors = Fukuda N, Emoto M, Nakamori Y, Taguchi A, Miyamoto S, Uraki S, Oka Y, Tanizawa Y | title = DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes | journal = Diabetes | volume = 58 | issue = 2 | pages = 377–84 | date = Feb 2009 | pmid = 19033398 | pmc = 2628611 | doi = 10.2337/db08-0303 }}</ref> [chromaffin cell](/source/chromaffin_cell)s of the [adrenal gland](/source/adrenal_gland)<ref name="pmid18596155">{{cite journal | vauthors = Friedrich R, Groffen AJ, Connell E, van Weering JR, Gutman O, Henis YI, Davletov B, Ashery U | title = DOC2B acts as a calcium switch and enhances vesicle fusion | journal = J Neurosci | volume = 28 | issue = 27 | pages = 6794–806 | date = Jul 2008 | pmid = 18596155 | pmc = 2673511 | doi = 10.1523/JNEUROSCI.0538-08.2008 }}</ref> and [beta cells](/source/beta_cells) in the pancreas.<ref name="pmid19410553">{{cite journal | vauthors = Miyazaki M, Emoto M, Fukuda N, Hatanaka M, Taguchi A, Miyamoto S, Tanizawa Y | title = DOC2b is a SNARE regulator of glucose-stimulated delayed insulin secretion | journal = Biochem Biophys Res Commun | volume = 384 | issue = 4 | pages = 461–5 | date = Jul 2009 | pmid = 19410553 | doi = 10.1016/j.bbrc.2009.04.133 }}</ref> In the central nervous system, Doc2b contributes to the spontaneous release of [neurotransmitters](/source/neurotransmitters), which was thought to be acting as a high-affinity Ca<sup>2+</sup> sensor for exocytosis of [synaptic vesicles](/source/synaptic_vesicles)<ref name="pmid20150444">{{cite journal | vauthors = Groffen AJ, Martens S, Díez Arazola R, Cornelisse LN, Lozovaya N, de Jong AP, Goriounova NA, Habets RL, Takai Y, Borst JG, Brose N, McMahon HT, Verhage M | title = Doc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter release | journal = Science | volume = 327 | issue = 5973 | pages = 1614–8 | date = Mar 2010 | pmid = 20150444 | pmc = 2846320 | doi = 10.1126/science.1183765 }}</ref>  However, further work has shown that while DOC2b is both important for spontaneous exocytosis of [synaptic vesicles](/source/synaptic_vesicles) and binds [Calcium](/source/Calcium), it does not in fact change the calcium dependence of spontaneous [synaptic vesicle](/source/synaptic_vesicle) release and thus can not be the calcium sensor for this process.<ref>*{{cite journal | vauthors = Pang ZP, Bacaj T, Yang X, Zhou P, Xu W, Südhof TC | title = Doc2 supports spontaneous synaptic transmission by a Ca2+-independent mechanism | journal = Neuron | volume = 70 | issue = 2 | pages = 244–251 | year = 2011 | pmid = 21521611 | doi = 10.1016/j.neuron.2011.03.011 | pmc=3102832}}</ref>

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal | vauthors = Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH | title = 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 | journal = Am. J. Hum. Genet. | volume = 72 | issue = 4 | pages = 918–30 | year = 2003 | pmid = 12621583 | pmc = 1180354 | doi = 10.1086/374320 }} 
*{{cite journal | vauthors = Duncan RR, Betz A, Shipston MJ, Brose N, Chow RH | title = Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo | journal = J. Biol. Chem. | volume = 274 | issue = 39 | pages = 27347–50 | year = 1999 | pmid = 10488064 | doi = 10.1074/jbc.274.39.27347 | doi-access = free }}
*{{cite journal | vauthors = Nagano F, Orita S, Sasaki T, Naito A, Sakaguchi G, Maeda M, Watanabe T, Kominami E, Uchiyama Y, Takai Y | title = Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport | journal = J. Biol. Chem. | volume = 273 | issue = 46 | pages = 30065–8 | year = 1998 | pmid = 9804756 | doi = 10.1074/jbc.273.46.30065 | doi-access = free }}
*{{cite journal | vauthors = Orita S, Naito A, Sakaguchi G, Maeda M, Igarashi H, Sasaki T, Takai Y | title = Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery | journal = J. Biol. Chem. | volume = 272 | issue = 26 | pages = 16081–4 | year = 1997 | pmid = 9195900 | doi = 10.1074/jbc.272.26.16081 | doi-access = free }}
*{{cite journal | vauthors = Verhage M, de Vries KJ, Røshol H, Burbach JP, Gispen WH, Südhof TC | title = DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion | journal = Neuron | volume = 18 | issue = 3 | pages = 453–61 | year = 1997 | pmid = 9115738 | doi = 10.1016/S0896-6273(00)81245-3 | s2cid = 17948539 | doi-access = free }}
*{{cite journal | vauthors = Kojima T, Fukuda M, Aruga J, Mikoshiba K | title = Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta) | journal = J. Biochem. | volume = 120 | issue = 3 | pages = 671–6 | year = 1997 | pmid = 8902635 | doi = 10.1093/oxfordjournals.jbchem.a021464 | doi-access = free }}
*{{cite journal | vauthors = Sakaguchi G, Orita S, Maeda M, Igarashi H, Takai Y | title = Molecular cloning of an isoform of Doc2 having two C2-like domains | journal = Biochem. Biophys. Res. Commun. | volume = 217 | issue = 3 | pages = 1053–61 | year = 1996 | pmid = 8554557 | doi = 10.1006/bbrc.1995.2876 }}
*{{cite journal | vauthors = Pang ZP, Bacaj T, Yang X, Zhou P, Xu W, Südhof TC | title = Doc2 supports spontaneous synaptic transmission by a Ca2+-independent mechanism | journal = Neuron | volume = 70 | issue = 2 | pages = 244–251 | year = 2011 | pmid = 21521611 | doi = 10.1016/j.neuron.2011.03.011 | pmc=3102832}}
{{refend}}

---
Adapted from the Wikipedia article [DOC2B](https://en.wikipedia.org/wiki/DOC2B) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/DOC2B?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.
