Biology:CACNG2
 Generic protein structure example |
Calcium channel, voltage-dependent, gamma subunit 2, also known as CACNG2 or stargazin is a protein that in humans is encoded by the CACNG2 gene.[1]
Function
L-type calcium channels are composed of five subunits. The protein encoded by this gene represents one of these subunits, gamma, and is one of several gamma subunit proteins. It is an integral membrane protein that is thought to stabilize the calcium channel in an inactive (closed) state. This protein is similar to the mouse stargazin protein, mutations in which having been associated with absence seizures, also known as petit-mal or spike-wave seizures. This gene is a member of the neuronal calcium channel gamma subunit gene subfamily of the PMP-22/EMP/MP20 family.[1]
Stargazin is involved in the transportation of AMPA receptors to the synaptic membrane, and the regulation of their receptor rate constants — via its extracellular domain — once it is there. As it is highly expressed throughout the cerebral cortex, it is likely to have an important role in learning within these areas, due to the importance of AMPA receptors in LTP.
Clinical significance
Disruptions of CACNG2 have been implicated in autism.[2]
Interactions
CACNG2 has been shown to interact with GRIA4,[3] DLG4,[3][4] and MAGI2.[5]
See also
- Voltage-dependent calcium channel
References
- ↑ 1.0 1.1 "Entrez Gene: CACNG2 calcium channel, voltage-dependent, gamma subunit 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10369.
- ↑ Brandler, William M.; Antaki, Danny; Gujral, Madhusudan; Noor, Amina; Rosanio, Gabriel; Chapman, Timothy R. et al. (24 March 2016). "Frequency and Complexity of De Novo Structural Mutation in Autism". The American Journal of Human Genetics 98 (4): 667–679. doi:10.1016/j.ajhg.2016.02.018. PMID 27018473.
- ↑ 3.0 3.1 "Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms". Nature 408 (6815): 936–43. 2000. doi:10.1038/35050030. PMID 11140673. Bibcode: 2000Natur.408..936C.
- ↑ "Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD-95". The Journal of Biological Chemistry 277 (14): 12359–63. Apr 2002. doi:10.1074/jbc.M200528200. PMID 11805122.
- ↑ "Stargazin and other transmembrane AMPA receptor regulating proteins interact with synaptic scaffolding protein MAGI-2 in brain". The Journal of Neuroscience 26 (30): 7875–84. Jul 2006. doi:10.1523/JNEUROSCI.1851-06.2006. PMID 16870733.
Further reading
- "Molecular characterization of the gene encoding the gamma subunit of the human skeletal muscle 1,4-dihydropyridine-sensitive Ca2+ channel (CACNLG), cDNA sequence, gene structure, and chromosomal location". The Journal of Biological Chemistry 268 (13): 9275–9. May 1993. doi:10.1016/S0021-9258(18)98346-8. PMID 8387489.
- "Identification and cloning of putative human neuronal voltage-gated calcium channel gamma-2 and gamma-3 subunits: neurologic implications". Mayo Clinic Proceedings 74 (4): 357–61. Apr 1999. doi:10.4065/74.4.357. PMID 10221464.
- "Genetic localization of the Ca2+ channel gene CACNG2 near SCA10 on chromosome 22q13". Epilepsia 41 (1): 24–7. Jan 2000. doi:10.1111/j.1528-1157.2000.tb01500.x. PMID 10643919.
- "Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms". Nature 408 (6815): 936–43. 2001. doi:10.1038/35050030. PMID 11140673. Bibcode: 2000Natur.408..936C.
- "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family". Genomics 71 (3): 339–50. Feb 2001. doi:10.1006/geno.2000.6440. PMID 11170751.
- "Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD-95". The Journal of Biological Chemistry 277 (14): 12359–63. Apr 2002. doi:10.1074/jbc.M200528200. PMID 11805122.
- "Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number". Proceedings of the National Academy of Sciences of the United States of America 99 (21): 13902–7. Oct 2002. doi:10.1073/pnas.172511199. PMID 12359873. Bibcode: 2002PNAS...9913902S.
- "Human neuronal stargazin-like proteins, gamma2, gamma3 and gamma4; an investigation of their specific localization in human brain and their influence on CaV2.1 voltage-dependent calcium channels expressed in Xenopus oocytes". BMC Neuroscience 4: 23. Sep 2003. doi:10.1186/1471-2202-4-23. PMID 14505496.
- "Dynamic interaction of stargazin-like TARPs with cycling AMPA receptors at synapses". Science 303 (5663): 1508–11. Mar 2004. doi:10.1126/science.1090262. PMID 15001777. Bibcode: 2004Sci...303.1508T.
- "A genome annotation-driven approach to cloning the human ORFeome". Genome Biology 5 (10): R84. 2005. doi:10.1186/gb-2004-5-10-r84. PMID 15461802.
- "A novel action of stargazin as an enhancer of AMPA receptor activity". Neuroscience Research 50 (4): 369–74. Dec 2004. doi:10.1016/j.neures.2004.10.002. PMID 15567474.
- "Stargazin reduces desensitization and slows deactivation of the AMPA-type glutamate receptors". The Journal of Neuroscience 25 (10): 2682–6. Mar 2005. doi:10.1523/JNEUROSCI.4834-04.2005. PMID 15758178.
- "Uncovering quantitative protein interaction networks for mouse PDZ domains using protein microarrays". Journal of the American Chemical Society 128 (17): 5913–22. May 2006. doi:10.1021/ja060943h. PMID 16637659.
- "Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics". The Journal of Biological Chemistry 281 (33): 23908–21. Aug 2006. doi:10.1074/jbc.M600679200. PMID 16793768.
- "Stargazin interaction with alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors is critically dependent on the amino acid at the narrow constriction of the ion channel". The Journal of Biological Chemistry 282 (26): 18758–66. Jun 2007. doi:10.1074/jbc.M611182200. PMID 17483093.
External links
- CACNG2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- CACNG2 human gene location in the UCSC Genome Browser.
- CACNG2 human gene details in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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