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Gene Review: 

DOC2A  -  double C2-like domains, alpha

Homo sapiens

Synonyms: Doc2, Doc2-alpha, Double C2-like domain-containing protein alpha
 
 
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Disease relevance of DOC2A

 

High impact information on DOC2A

  • DOC2A was virtually brain specific, DOC2B ubiquitous [2].
  • Doc2 has one Munc13-interacting domain at the N-terminal region and two C2-like domains interacting with Ca2+ and phospholipid at the C-terminal region [3].
  • Overexpression of the C-terminal fragment containing two C2-like domains shows the similar effect, but to a lesser extent, whereas overexpression of full-length Doc2 or the C-terminal fragment of rabphilin3 containing two C2-like domains does not show this effect [3].
  • Because dynein is a minus-end-directed microtubule-based motor protein, these results suggest that Doc2, especially Doc2beta, plays a role in dynein-dependent intracellular vesicle transport [3].
  • Overexpression of the N-terminal fragment of Doc2 containing the tctex-1-interacting domain induces changes in the intracellular localization of cation-independent mannose 6-phosphate receptor and its ligand, cathepsin D, which are transported from trans-Golgi network to late endosomes [3].
 

Biological context of DOC2A

  • Overexpression of the Doc2-interacting domain of Munc13 reduces the Ca2+-dependent exocytosis from PC12 cells, and co-expression with Doc2 suppresses this reduction [4].
 

Anatomical context of DOC2A

 

Associations of DOC2A with chemical compounds

  • To identify calcium sensors involved in this signalling, we investigated soluble C2 domain-containing proteins and found that both DOC2A and DOC2B are modulated by submicromolar calcium levels [5].
  • The Doc2-Munc13 interactions are stimulated by phorbol ester through the C1 domain of Munc13 [4].
 

Analytical, diagnostic and therapeutic context of DOC2A

References

  1. Doc-2/hDab2 expression is up-regulated in primary pancreatic cancer but reduced in metastasis. Huang, Y., Friess, H., Kleeff, J., Esposito, I., Zhu, Z., Liu, S., Mok, S.C., Zimmermann, A., Büchler, M.W. Lab. Invest. (2001) [Pubmed]
  2. DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion. Verhage, M., de Vries, K.J., Røshol, H., Burbach, J.P., Gispen, W.H., Südhof, T.C. Neuron (1997) [Pubmed]
  3. Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport. Nagano, F., Orita, S., Sasaki, T., Naito, A., Sakaguchi, G., Maeda, M., Watanabe, T., Kominami, E., Uchiyama, Y., Takai, Y. J. Biol. Chem. (1998) [Pubmed]
  4. Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery. Orita, S., Naito, A., Sakaguchi, G., Maeda, M., Igarashi, H., Sasaki, T., Takai, Y. J. Biol. Chem. (1997) [Pubmed]
  5. DOC2A and DOC2B are sensors for neuronal activity with unique calcium-dependent and kinetic properties. Groffen, A.J., Friedrich, R., Brian, E.C., Ashery, U., Verhage, M. J. Neurochem. (2006) [Pubmed]
  6. Doc2: a novel brain protein having two repeated C2-like domains. Orita, S., Sasaki, T., Naito, A., Komuro, R., Ohtsuka, T., Maeda, M., Suzuki, H., Igarashi, H., Takai, Y. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  7. Molecular cloning of an isoform of Doc2 having two C2-like domains. Sakaguchi, G., Orita, S., Maeda, M., Igarashi, H., Takai, Y. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
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