149
Oocytes and Receptors and Channels
Hassaine, G., C. Deluz, L. Grasso, R. Wyss, M. B. Tol, R. Hovius,
A. Graff, H. Stahlberg, T. Tomizaki, A. Desmyter, C. Moreau,
X. D. Li, F. Poitevin, H. Vogel, H. Nury. 2014. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature 512:276–
281. https://doi.org/10.1038/nature13552 .
Hershey, A. D., L. Polenzani, R. M. Woodward, R. Miledi, and
J. E. Krause. 1991. Molecular and genetic characterization,
functional expression, and mRNA expression patterns of a
rat substance P receptor. Annals of the New York Academy
of Sciences 632:63–73. https://doi.org/10.1111/j.1749-6632.
1991.tb33095.x.
Hou, P., J. Shi, K. M. White, Y. Gao, and J. Cui. 2019. ML277 specifcally enhances the fully activated open state of KCNQ1
by modulating VSD-pore coupling. Elife 8:e48576. https://
doi.org/10.7554/eLife.48576 .
Huang, Y., R. Fliegert, A. H. Guse, W. Lü, and J. Du. 2020. A
structural overview of the ion channels of the TRPM family. Cell Calcium 85:102111. https://doi.org/10.1016/j.ceca.
2019.102111 .
Kalani, M. Y., A. S. Filippidis, and H. L. Rekate. 2012.
Hydrocephalus and aquaporins: The role of aquaporin-1.
Acta Neurochirurgica Supplement 113:51–54. https://doi.
org/10.1007/978-3-7091-0923-6_11.
Kelly, J. J., J. L. Esseltine, Q. Shao, E. W. Jabs, J. Sampson, M.
Auranen, D. Bai, and D. W. Laird. 2016. Specif c functional
pathologies of Cx43 mutations associated with oculodentodigital dysplasia. Molecular of Biology Cell 27:2172–2185.
https://doi.org/10.1091/mbc.E16-01-0062 .
Kesters, D., A. J. Thompson, M. Brams, R. van Elk, R. Spurny,
M. Geitmann, J. M. Villalgordo, A. Guskov, U. H. Danielson,
S. C. Lummis, A. B. Smit, and C. Ulens. 2013. Structural
basis of ligand recognition in 5-HT3 receptors. The EMBO
Journal 14:49–56. https://doi.org/10.1038/embor.2012.189 .
Kim, J. C., M. Pérez-Hernández, F. J. Alvarado, S. R. Maurya, J.
Montnach, Y. Yin, M. Zhang, X. Lin, C. Vasquez, A. Heguy,
F. X. Liang, S. H. Woo, G. E. Morley, E. Rothenberg,
A. Lundby, H. H. Valdivia, M. Cerrone, and M. Delmar.
2019. Disruption of Ca2+i homeostasis and connexin 43
hemichannel function in the right ventricle precedes overt
arrhythmogenic cardiomyopathy in plakophilin-2-def cient
mice. Circulation 140:1015–1030. https://doi.org/10.1161/
CIRCULATIONAHA.119.039710 .
Kuhse, J., V. Schmieden, and H. Betz. 1990. Identif cation and
functional expression of a novel ligand binding subunit of the
inhibitory glycine receptor. Journal of Biological Chemistry
265:22317–22320.
Kusano, K, R. Miledi, and J. Stinnakre. 1977. Acetylcholine receptors in the oocyte membrane. Nature 270:22–29.
Lane, C. D., G. Marbaix, and J. B. Gurdon. 1971. Rabbit haemoglobin synthesis in frog cells: The translation of reticulocyte
9 s RNA in frog oocytes. Journal of Molecular and Biology
61:73–91. https://doi.org/10.1016/0022-2836(71)90207-5 .
Limon, A., J. M. Reyes-Ruiz, and R. Miledi. 2008. Microtransplantation of neurotransmitter receptors from postmortem
autistic brains to Xenopus oocytes. Proceedings of the National
Academy of Sciences 105:10973–10977. https://doi.org/10.
1073/pnas.0804386105 .
Macari, F., M. Landau, P. Cousin, B. Mevorah, S. Brenner,
R. Panizzon, D. F. Schorderet, D. Hohl, and M. Huber.
2000. Mutation in the gene for connexin 30.3 in a family with erythrokeratodermia variabilis. American Journal
Human Genetics 67:1296–1301. https://doi.org/10.1016/
S0002-9297(07)62957-7 .
Mackinnon, R., P. H. Reinhart, and M. M. White. 1988. Charybdotoxin
block of Shaker K+ channels suggests that different types
of K+ channels share common structural features. Neuron
1:997–1001. https://doi.org/10.1016/0896-6273(88)90156-0 .
Maricq, A. V., A. S. Peterson, A. J. Brake, R. M. Myers, and D.
Julius. 1991. Primary structure and functional expression of
the 5HT3 receptor, a serotonin-gated ion channel. Science
254:432–4337. https://doi.org/10.1126/science.1718042 .
McCray, B. A., A. Schindler, J. E. Hoover-Fong, and C. J. Sumner.
2014. Autosomal dominant TRPV4 disorders. GeneReviews.
www.ncbi.nlm.nih.gov/books/NBK201366/ .
Miledi, R. 1982. A calcium-dependent transient outward current in
Xenopus laevis oocytes. Proceedings of the Royal Society of
London: Series B, Biological Sciences 215:491–497. https://
doi.org/10.1098/rspb.1982.0056.
Miledi, R., Z. Dueñas, A. Martínez-Torres, C. H. Kawas, and F.
Eusebi. 2004. Microtransplantation of functional receptors
and channels from the Alzheimer’s brain to frog oocytes.
Proceedings of the National Academy of Sciences 101:1760–
1763. https://doi.org/10.1073/pnas.0308224100 .
Miledi, R., F. Eusebi, A. Martínez-Torres, E. Palma, and F. Trettel.
2002. Expression of functional neurotransmitter receptors in
Xenopus oocytes after injection of human brain membranes.
Proceedings of the National Academy of Sciences 99:13238–
13942. https://doi.org/10.1073/pnas.192445299 .
Miledi, R., and I. Parker. 1984. Chloride current induced by injection of calcium into Xenopus oocytes. Journal of Physiology
357:173–183. https://doi.org/10.1113/jphysiol.1984.sp015495 .
Miledi, R., I. Parker, and K. Sumikawa. 1982. Properties of acetylcholine receptors translated by cat muscle mRNA in Xenopus
oocytes. The EMBO Journal 1:1307–1312.
Miledi, R., I. Parker, and K. Sumikawa. 1983. Recording of single
gamma-aminobutyrate-and acetylcholine-activated receptor channels translated by exogenous mRNA in Xenopus
oocytes. Proceedings of the Royal Society of London: Series
B, Biological Sciences 218:481–484. https://doi.org/10.1098/
rspb.1983.0053.
Miledi, R., I, Parker, and R. M. Woodward. 1989. Membrane
currents elicited by divalent cations in Xenopus oocytes.
Journal of Physiology 417:173–195. https://doi.org/10.1113/
jphysiol.1989.sp017796 .
Miledi, R., and R. M. Woodward. 1989a. Membrane currents elicited by prostaglandins, atrial natriuretic factor and oxytocin
in follicle-enclosed Xenopus oocytes. Journal of Physiology
416:623–643. https://doi.org/10.1113/jphysiol.1989.sp017781 .
Miledi, R., and R. M. Woodward. 1989b. Effects of defolliculation
on membrane current responses of Xenopus oocytes. Journal
of Physiology 416:601–621.
Miller, P. S., and A. S. Aricescu. 2014. Crystal structure of a
human GABAA receptor. Nature 512:270–275. https://doi.
org/10.1038/nature13293.
Murai, T., A. Kakizuka, T.Takumi, H. Ohkubo, and S. Nakanishi. 1989.
Molecular cloning and sequence analysis of human genomic
DNA encoding a novel membrane protein which exhibits a
slowly activating potassium channel activity. Biochemical
and Biophysical Research Communications 161:176–181.
https://doi.org/10.1016/0006-291x(89)91577-5 .
Nagahara, M., Y. Waguri-Nagaya, T. Yamagami, M. Aoyama, T.
Tada, K. Inoue, K. Asai, and T. Otsuka. 2010. TNF-alphainduced aquaporin 9 in synoviocytes from patients with OA
and RA. Rheumatology 49:898–906. https://doi.org/10.1093/
rheumatology/keq028.
Nikolic, Z., B. Laube, R. G. Weber, P. Lichter, P. Kioschis,
A. Poustka, C. Mülhardt, and C. M. Becker. 1998. The
human glycine receptor subunit alpha3: Glra3 gene structure, chromosomal localization, and functional characterization of alternative transcripts. Journal of Biological
Oocytes and Receptors and Channels
Hassaine, G., C. Deluz, L. Grasso, R. Wyss, M. B. Tol, R. Hovius,
A. Graff, H. Stahlberg, T. Tomizaki, A. Desmyter, C. Moreau,
X. D. Li, F. Poitevin, H. Vogel, H. Nury. 2014. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature 512:276–
281. https://doi.org/10.1038/nature13552 .
Hershey, A. D., L. Polenzani, R. M. Woodward, R. Miledi, and
J. E. Krause. 1991. Molecular and genetic characterization,
functional expression, and mRNA expression patterns of a
rat substance P receptor. Annals of the New York Academy
of Sciences 632:63–73. https://doi.org/10.1111/j.1749-6632.
1991.tb33095.x.
Hou, P., J. Shi, K. M. White, Y. Gao, and J. Cui. 2019. ML277 specifcally enhances the fully activated open state of KCNQ1
by modulating VSD-pore coupling. Elife 8:e48576. https://
doi.org/10.7554/eLife.48576 .
Huang, Y., R. Fliegert, A. H. Guse, W. Lü, and J. Du. 2020. A
structural overview of the ion channels of the TRPM family. Cell Calcium 85:102111. https://doi.org/10.1016/j.ceca.
2019.102111 .
Kalani, M. Y., A. S. Filippidis, and H. L. Rekate. 2012.
Hydrocephalus and aquaporins: The role of aquaporin-1.
Acta Neurochirurgica Supplement 113:51–54. https://doi.
org/10.1007/978-3-7091-0923-6_11.
Kelly, J. J., J. L. Esseltine, Q. Shao, E. W. Jabs, J. Sampson, M.
Auranen, D. Bai, and D. W. Laird. 2016. Specif c functional
pathologies of Cx43 mutations associated with oculodentodigital dysplasia. Molecular of Biology Cell 27:2172–2185.
https://doi.org/10.1091/mbc.E16-01-0062 .
Kesters, D., A. J. Thompson, M. Brams, R. van Elk, R. Spurny,
M. Geitmann, J. M. Villalgordo, A. Guskov, U. H. Danielson,
S. C. Lummis, A. B. Smit, and C. Ulens. 2013. Structural
basis of ligand recognition in 5-HT3 receptors. The EMBO
Journal 14:49–56. https://doi.org/10.1038/embor.2012.189 .
Kim, J. C., M. Pérez-Hernández, F. J. Alvarado, S. R. Maurya, J.
Montnach, Y. Yin, M. Zhang, X. Lin, C. Vasquez, A. Heguy,
F. X. Liang, S. H. Woo, G. E. Morley, E. Rothenberg,
A. Lundby, H. H. Valdivia, M. Cerrone, and M. Delmar.
2019. Disruption of Ca2+i homeostasis and connexin 43
hemichannel function in the right ventricle precedes overt
arrhythmogenic cardiomyopathy in plakophilin-2-def cient
mice. Circulation 140:1015–1030. https://doi.org/10.1161/
CIRCULATIONAHA.119.039710 .
Kuhse, J., V. Schmieden, and H. Betz. 1990. Identif cation and
functional expression of a novel ligand binding subunit of the
inhibitory glycine receptor. Journal of Biological Chemistry
265:22317–22320.
Kusano, K, R. Miledi, and J. Stinnakre. 1977. Acetylcholine receptors in the oocyte membrane. Nature 270:22–29.
Lane, C. D., G. Marbaix, and J. B. Gurdon. 1971. Rabbit haemoglobin synthesis in frog cells: The translation of reticulocyte
9 s RNA in frog oocytes. Journal of Molecular and Biology
61:73–91. https://doi.org/10.1016/0022-2836(71)90207-5 .
Limon, A., J. M. Reyes-Ruiz, and R. Miledi. 2008. Microtransplantation of neurotransmitter receptors from postmortem
autistic brains to Xenopus oocytes. Proceedings of the National
Academy of Sciences 105:10973–10977. https://doi.org/10.
1073/pnas.0804386105 .
Macari, F., M. Landau, P. Cousin, B. Mevorah, S. Brenner,
R. Panizzon, D. F. Schorderet, D. Hohl, and M. Huber.
2000. Mutation in the gene for connexin 30.3 in a family with erythrokeratodermia variabilis. American Journal
Human Genetics 67:1296–1301. https://doi.org/10.1016/
S0002-9297(07)62957-7 .
Mackinnon, R., P. H. Reinhart, and M. M. White. 1988. Charybdotoxin
block of Shaker K+ channels suggests that different types
of K+ channels share common structural features. Neuron
1:997–1001. https://doi.org/10.1016/0896-6273(88)90156-0 .
Maricq, A. V., A. S. Peterson, A. J. Brake, R. M. Myers, and D.
Julius. 1991. Primary structure and functional expression of
the 5HT3 receptor, a serotonin-gated ion channel. Science
254:432–4337. https://doi.org/10.1126/science.1718042 .
McCray, B. A., A. Schindler, J. E. Hoover-Fong, and C. J. Sumner.
2014. Autosomal dominant TRPV4 disorders. GeneReviews.
www.ncbi.nlm.nih.gov/books/NBK201366/ .
Miledi, R. 1982. A calcium-dependent transient outward current in
Xenopus laevis oocytes. Proceedings of the Royal Society of
London: Series B, Biological Sciences 215:491–497. https://
doi.org/10.1098/rspb.1982.0056.
Miledi, R., Z. Dueñas, A. Martínez-Torres, C. H. Kawas, and F.
Eusebi. 2004. Microtransplantation of functional receptors
and channels from the Alzheimer’s brain to frog oocytes.
Proceedings of the National Academy of Sciences 101:1760–
1763. https://doi.org/10.1073/pnas.0308224100 .
Miledi, R., F. Eusebi, A. Martínez-Torres, E. Palma, and F. Trettel.
2002. Expression of functional neurotransmitter receptors in
Xenopus oocytes after injection of human brain membranes.
Proceedings of the National Academy of Sciences 99:13238–
13942. https://doi.org/10.1073/pnas.192445299 .
Miledi, R., and I. Parker. 1984. Chloride current induced by injection of calcium into Xenopus oocytes. Journal of Physiology
357:173–183. https://doi.org/10.1113/jphysiol.1984.sp015495 .
Miledi, R., I. Parker, and K. Sumikawa. 1982. Properties of acetylcholine receptors translated by cat muscle mRNA in Xenopus
oocytes. The EMBO Journal 1:1307–1312.
Miledi, R., I. Parker, and K. Sumikawa. 1983. Recording of single
gamma-aminobutyrate-and acetylcholine-activated receptor channels translated by exogenous mRNA in Xenopus
oocytes. Proceedings of the Royal Society of London: Series
B, Biological Sciences 218:481–484. https://doi.org/10.1098/
rspb.1983.0053.
Miledi, R., I, Parker, and R. M. Woodward. 1989. Membrane
currents elicited by divalent cations in Xenopus oocytes.
Journal of Physiology 417:173–195. https://doi.org/10.1113/
jphysiol.1989.sp017796 .
Miledi, R., and R. M. Woodward. 1989a. Membrane currents elicited by prostaglandins, atrial natriuretic factor and oxytocin
in follicle-enclosed Xenopus oocytes. Journal of Physiology
416:623–643. https://doi.org/10.1113/jphysiol.1989.sp017781 .
Miledi, R., and R. M. Woodward. 1989b. Effects of defolliculation
on membrane current responses of Xenopus oocytes. Journal
of Physiology 416:601–621.
Miller, P. S., and A. S. Aricescu. 2014. Crystal structure of a
human GABAA receptor. Nature 512:270–275. https://doi.
org/10.1038/nature13293.
Murai, T., A. Kakizuka, T.Takumi, H. Ohkubo, and S. Nakanishi. 1989.
Molecular cloning and sequence analysis of human genomic
DNA encoding a novel membrane protein which exhibits a
slowly activating potassium channel activity. Biochemical
and Biophysical Research Communications 161:176–181.
https://doi.org/10.1016/0006-291x(89)91577-5 .
Nagahara, M., Y. Waguri-Nagaya, T. Yamagami, M. Aoyama, T.
Tada, K. Inoue, K. Asai, and T. Otsuka. 2010. TNF-alphainduced aquaporin 9 in synoviocytes from patients with OA
and RA. Rheumatology 49:898–906. https://doi.org/10.1093/
rheumatology/keq028.
Nikolic, Z., B. Laube, R. G. Weber, P. Lichter, P. Kioschis,
A. Poustka, C. Mülhardt, and C. M. Becker. 1998. The
human glycine receptor subunit alpha3: Glra3 gene structure, chromosomal localization, and functional characterization of alternative transcripts. Journal of Biological
