Stevens, M. & Merilaita, S. Animal camouflage: mechanisms and function (eds. Martin, S. & Merilaita, S.) (Cambridge University Press, 2011).
Stevens, M. & Merilaita, S. Animal camouflage: current issues and new perspectives. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364(1516), 423–427, 10.1098/rstb.2008.0217 (2008). DOI: 10.1098/rstb.2008.0217
Körner, H. K. Countershading by physiological colour change in the fish louse Anilocra physodes L. (Crustacea: Isopoda). Oceologia 55(2), 248–250, 10.1007/BF00384495 (1982). DOI: 10.1007/BF00384495
Allen, W. L., Baddeley, R., Cuthill, I. C. & Scott-samuel, N. E. A quantitative test of the predicted relationship between countershading and lighting environment. Am. Nat. 180(6), 762–776, 10.1086/668011 (2012). DOI: 10.1086/668011
Edmunds, M. & Dewhirst, R. A. The survival value of countershading with wild birds as predators. Biol. J. Linn. Soc. 51(4), 447–452, 10.1111/j.1095-8312.1994.tb00973.x (1994). DOI: 10.1111/j.1095-8312.1994.tb00973.x
Hadley, M. C. & Goldman, J. M. Physiological color changes in reptiles. Integr. Comp. Biol. 9(2), 489–504, 10.1093/icb/9.2.489 (1969). DOI: 10.1093/icb/9.2.489
Rozdzial, M. M. & Haimo, L. T. Bidirectional pigment granule movements of melanophores are regulated by protein phosphorylation and dephosphorylation. Cell. 47(6), 1061–1070, 10.1016/0092-8674(86)90821-4 (1986). DOI: 10.1016/0092-8674(86)90821-4
Sherbrooke, W. C. Physiological (rapid) change of color in horned lizards. Amphibia-Reptilia 18(2), 155–175, 10.1163/156853897X00044 (1997). DOI: 10.1163/156853897X00044
Visconti, M. A., Ramanzini, G. C., Camargo, C. R. & Castrucci, A. M. L. Elasmobranch color change: A short review and novel data on hormone regulation. J. Exp. Zool. 284(5), 485–491, 10.1002/(SICI)1097-010X(19991001)284:5<485::AID-JEZ3>3.0.CO;2-5 (1999). DOI: 10.1002/(SICI)1097-010X(19991001)284:5<485::AID-JEZ3>3.0.CO;2-5
Gross, S. P. et al. Interactions and regulation of molecular motors in Xenopus melanophores. J. Cell Biol. 156(5), 855, 10.1083/jcb.200105055 (2002). DOI: 10.1083/jcb.200105055
Logan, D. W., Burn, S. F. & Jackson, I. J. Regulation of pigmentation in zebrafish melanophores. Pigment Cell Res. 19(3), 206–213, 10.1111/j.1600-0749.2006.00307.x (2006). DOI: 10.1111/j.1600-0749.2006.00307.x
Tuma, M. C. & Gelfand, V. I. Molecular mechanisms of pigment transport in melanophores. Pigment Cell Melanoma Res. 12(5), 283–294, 10.1111/j.1600-0749.1999.tb00762.x (2006). DOI: 10.1111/j.1600-0749.1999.tb00762.x
Leclercq, E., Taylor, J. F. & Migaud, H. Morphological skin colour changes in teleosts. Fish and Fisheries 11(2), 159–193, 10.1111/j.1467-2979.2009.00346.x (2010). DOI: 10.1111/j.1467-2979.2009.00346.x
Sköld, H. N., Aspengren, S. & Wallin, M. Rapid color change in fish and amphibians – function, regulation and emerging applications. Pigment Cell Melanoma Res. 26(1), 29–38, 10.1111/pcmr.12040 (2012). DOI: 10.1111/pcmr.12040
Kelley, J. L. & Davies, W. I. L. The biological mechanisms and behavioral functions of opsin-based light detection by the skin. Front. Ecol. Evol. 4, 106, 10.3389/fevo.2016.00106 (2016). DOI: 10.3389/fevo.2016.00106
Regazzetti, C. et al. Melanocytes sense blue light and regulate pigmentation through opsin-3. J. Investig. Dermatol. 138(1), 171–178, 10.1016/j.jid.2017.07.833 (2018). DOI: 10.1016/j.jid.2017.07.833
Schliwa, M. & Bereiter-Hahn, J. Pigment movements in fish melanophores: Morphological and physiological studies. J. Cell Tissue Res. 151(4), 423–432, 10.1007/BF00219951 (1974). DOI: 10.1007/BF00219951
Obika, M., Menter, D. G., Tchen, T. T. & Taylor, J. D. Actin microfilaments in melanophores of Fundulus heteroclitus. J. Cell Tissue Res. 193(3), 387–397, 10.1007/BF00225337 (1978). DOI: 10.1007/BF00225337
McNiven, M. A., Wang, M. & Porter, K. R. Microtubule polarity and the direction of pigment transport reverse simultaneously in surgically severed melanophore arms. Cell. 37(3), 753–765, 10.1016/0092-8674(84)90411-2 (1984). DOI: 10.1016/0092-8674(84)90411-2
Schliwa, M. Pigment Cells in Biology of the Integument: 2 Vertebrates (eds. Bereiter-Hahn, J., Matolsy, A. G. & Richards, K. S.) 65–77 (Berlin, Heidelberg, Springer Berlin Heidelberg, 1986).
Hanlon, R., et al Cephalopod dynamic camouflage: bridging the continuum between background matching and disruptive coloration. Philos. Trans. Royal Soc. B. 364(1516), https://doi.org/10.1098/rstb.2008.0270 (2008).
Chiao, C. C., Wickiser, J. K., Allen, J. J., Genter, B. & Hanlon, R. Hyperspectral imaging of cuttlefish camouflage indicates good color match in the eyes of fish predators. Proc. Natl. Acad. Sci. USA 108(22), 9148–9153, 10.1073/pnas.1019090108 (2011). DOI: 10.1073/pnas.1019090108
Hanlon, R., et al Rapid adaptive camouflage in cephalopods in Animal camouflage: mechanisms and functions (eds. Martin, S. & Merilaita, S.) 145–163 (Cambridge University Press, 2011).
Zylinski, S. & Johnsen, S. Mesopelagic cephalopods switch between transparency and pigmentation to optimize camouflage in the deep. Curr. Biol. 21(22), 1937–1941, 10.1016/j.cub.2011.10.014 (2011). DOI: 10.1016/j.cub.2011.10.014
Ramachandran, V. S. et al. Rapid adaptive camouflage in tropical flounders. Nature. 379(6568), 815–818, 10.1038/379815a0 (1996). DOI: 10.1038/379815a0
Marshall, N. J. Communication and camouflage with the same ‘bright’colours in reef fishes. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355(1401), 1243–1248, 10.1098/rstb.2000.0676 (2000). DOI: 10.1098/rstb.2000.0676
Marshall, J. & Johnsen, S. Camouflage in marine fish in Animal Camouflage: Mechanisms and Function (eds. Martin, S. & Merilaita, S.) 186–211 (Cambridge University Press, 2011).
Heithaus, M. R., Dill, L. M., Marshall, G. J. & Buhleier, B. Habitat use and foraging behavior of tiger sharks (Galeocerdo cuvier) in a seagrass ecosystem. Mar. Biol. 140, 237–248, 10.1007/s00227-001-0711-7 (2002). DOI: 10.1007/s00227-001-0711-7
Clarke, G. L. & Backus, R. H. Measurements of light penetration in relation to vertical migration and records of luminescence of deep-sea animals. Deep Sea Res. 4, 1–14, 10.1016/0146-6313(56)90026-0 (1957). DOI: 10.1016/0146-6313(56)90026-0
Duntley, S. Q. Light in the sea. J. Opt. Soc. Am. 53(2), 214–233, 10.1364/JOSA.53.000214 (1963). DOI: 10.1364/JOSA.53.000214
Aksnes, D. L. et al. Light penetration structures the deep acoustic scattering layers in the global ocean. Sci. Adv. 3(5), e1602468, 10.1126/sciadv.1602468 (2017). DOI: 10.1126/sciadv.1602468
Hastings, J. W. Light to hide by: ventral luminescence to camouflage the silhouette. Science. 173(4001), 1016–1017, 10.1126/science.173.4001.1016 (1971). DOI: 10.1126/science.173.4001.1016
Denton, E. J., Gilpin-Brown, J. B. & Wright, P. G. The angular distribution of the light produced by some mesopelagic fish in relation to their camouflage. Proc. R. Soc. Lond. B Biol. Sci. 182(1067), 145–158, 10.1098/rspb.1972.0071 (1972). DOI: 10.1098/rspb.1972.0071
Young, R. E. & Roper, C. F. Bioluminescent countershading in midwater animals: evidence from living squid. Science. 191(4231), 1046–1048, 10.1126/science.1251214 (1976). DOI: 10.1126/science.1251214
McFall-Ngai, M. & Morin, J. G. Camouflage by disruptive illumination in Leiognathids, a family of shallow-water, bioluminescent fishes. J. Exp. Biol. 156(1), 119–137 (1991).
Dahlgren, U. The production of light by animals. J. Franklin Inst. 181(5), 659–696, 10.1016/S0016-0032(16)90625-2 (1917). DOI: 10.1016/S0016-0032(16)90625-2
Fraser, J. H. Nature adrift (1962).
Clarke, W. D. Function of bioluminescence in mesopelagic organisms. Nature. 198(4887), 1244, 10.1038/1981244a0 (1963). DOI: 10.1038/1981244a0
McAllister, D. E. The significance of ventral bioluminescence in fishes. Journal of the Fisheries Board of Canada 24(3), 537–554, 10.1139/f67-047 (1967). DOI: 10.1139/f67-047
Straube, N., Iglésias, S. P., Sellos, D. Y., Kriwet, J. & Schliewen, U. K. Molecular phylogeny and node time estimation of bioluminescence lantern sharks (Elasmobranchii: Etmopteridae). Mol. Phylogenet. Evol. 56(3), 905–917, 10.1016/j.ympev.2010.04.042 (2010). DOI: 10.1016/j.ympev.2010.04.042
Straube, N., Li, C., Claes, J. M., Corrigan, S. & Naylor, G. J. P. Molecular phylogeny of Squaliformes and first occurrence of bioluminescence in sharks. BMC Evol. Biol. 15(1), 162, 10.1186/s12862-015-0446-6 (2015). DOI: 10.1186/s12862-015-0446-6
Claes, J. M. & Mallefet, J. Bioluminescence of sharks: first synthesis (ed. Meyer-Rochow, V. B.) 51–65 (Research Signpost, 2009).
Claes, J. M. & Mallefet, J. Hormonal control of luminescence from lantern shark (Etmopterus spinax) photophores. J. Exp. Biol. 212(22), 3684–3692, 10.1242/jeb.034363 (2009). DOI: 10.1242/jeb.034363
Claes, J. M. & Mallefet, J. Comparative control of luminescence in sharks: new insights from the slendertail lanternshark (Etmopterus molleri). J. Exp. Mar. Biol. Ecol. 467, 87–94, 10.1016/j.jembe.2015.03.008 (2015). DOI: 10.1016/j.jembe.2015.03.008
Claes, J. M., Sato, K. & Mallefet, J. Morphology and control of photogenic structures in a rare dwarf pelagic lantern shark (Etmopterus splendidus). J. Exp. Mar. Biol. Ecol. 406(1-2), 1–5, 10.1016/j.jembe.2011.05.033 (2011). DOI: 10.1016/j.jembe.2011.05.033
Claes, J. M., Nilsson, D.-E., Straube, N., Collin, S. P. & Mallefet, J. Iso-luminance counterillumination drove bioluminescent shark radiation. Sci. Rep. 4, 4328, 10.1038/srep04328 (2014). DOI: 10.1038/srep04328
Duchatelet, L., et al Adrenocorticotropic hormone and cyclic adenosine monophosphate are involved in the control of shark bioluminescence. Photochem. Photobiol., 10.1111/php.13154 (2020).
Duchatelet, L., Pinte, N., Tomita, T., Sato, K. & Mallefet, J. Etmopteridae bioluminescence: dorsal pattern specificity and aposematic use. Zool. Lett. 5, 9, 10.1186/s40851-019-0126-2 (2019). DOI: 10.1186/s40851-019-0126-2
Massuti, E. & Moranta, J. Demersal assemblages and depth distribution of elasmobranchs from the continental shelf and slope off the Balearic Islands (western Mediterranean). ICES J. Mar. Sci. 60, 753–766, 10.1016/S1054-3139(03)00089-4 (2003). DOI: 10.1016/S1054-3139(03)00089-4
Coelho, R. & Erzini, K. Depth distribution of the velvet belly, Etmopterus spinax, in relation to growth and reproductive cycle: the case study of a deep-water lantern shark with a wide-ranging critical habitat. Mar. Biol. Res. 6(4), 381–389, 10.1080/17451000802644706 (2010). DOI: 10.1080/17451000802644706
Straube, N., Kriwet, J. & Schliewen, U. K. Cryptic diversity and species assignment of large lantern sharks of the Etmopterus spinax clade from the Southern Hemisphere (Squaliformes, Etmopteridae). Zool. Scr. 40(1), 61–75, 10.1111/j.1463-6409.2010.00455.x (2011). DOI: 10.1111/j.1463-6409.2010.00455.x
Saad, A. & Alkusairy, H. Occurrence of mature female of Etmopterus spinax (Chondrichthyes: Etmopteridae) in the Syrian coast (Eastern Mediterranean). Ad. Oceanogr. & Marine Biol. 1(1), 504 (2018).
Klimpel, S., Palm, H. W. & Seehagen, A. Metazoan parasites and food composition of juvenile Etmopterus spinax (L., 1758) (Dalatiidae, Squaliformes) from the Norvegian deep. Parasitol. Res. 89(4), 245–251, 10.1007/s00436-002-0741-1 (2003). DOI: 10.1007/s00436-002-0741-1
Neiva, J., Coelho, R. & Erzini, K. Feeding habits of the velvet belly lanternshark Etmopterus spinax (Chondrichthyes: Etmopteridae) off Algarve, Southern Portugal. J. Mar. Biol. Assoc. UK 86(4), 835–841, 10.1017/S0025315406013762 (2006). DOI: 10.1017/S0025315406013762
Clarke, M. R. & Merret, N. The significance of squid, whale and other remains from the stomachs of bottom-living deep-sea fish. J. Mar. Biol. Assoc. UK 52(3), 599, 10.1017/S0025315400021603 (1972). DOI: 10.1017/S0025315400021603
Matallanas, J. Feeding habits of Scyliorhinus licha in Catalan waters. J. Fish Biol. 20, 155–163, 10.1111/j.1095-8649.1982.tb03916.x (1982). DOI: 10.1111/j.1095-8649.1982.tb03916.x
Santos, J. & Borges, T. Trophic relationships in deep-water fish communities off Algarve, Portugal. Fish. Res. 51(23), 337–341, 10.1016/S0165-7836(01)00257-0 (2001). DOI: 10.1016/S0165-7836(01)00257-0
Navarro, J., López, L., Coll, M., Barría, C. & Sáez-Liante, R. Short- and long-term importance of small sharks in the diet of the rare deep-sea shark Dalatias licha. Mar. Biol. 161, 1697–707, 10.1007/s00227-014-2454-2 (2014). DOI: 10.1007/s00227-014-2454-2
Claes, J. M., Aksnes, D. L. & Mallefet, J. Phantom hunter of the fjords: camouflage by counterillumination in a shark (Etmopterus spinax). J. Exp. Mar. Biol. Ecol. 388(1-2), 28–32, 10.1016/j.jembe.2010.03.009 (2010). DOI: 10.1016/j.jembe.2010.03.009
Claes, J. M. et al. Photon hunting in the twilight zone: visual features of mesopelagic bioluminescent sharks. PloS One 9(8), e104213, 10.1371/journal.pone.0104213 (2014). DOI: 10.1371/journal.pone.0104213
Finucci, B., Dunn, M. R. & Jones, E. G. Aggregations and associations in deep-sea chondrichthyans. ICES J. Mar. Sci. 75(5), 1613–1626, 10.1093/icesjms/fsy034 (2018). DOI: 10.1093/icesjms/fsy034
Coelho, R. & Erzini, K. Life history of a wide-ranging deep water lantern shark in the North-East Atlantic, Etmopterus spinax (Chondrichthyes: Etmopteridae), with implications for conservation. J. Fish Biol. 73(6), 1419–1443, 10.1111/j.1095-8649.2008.02021.x (2008). DOI: 10.1111/j.1095-8649.2008.02021.x
Gennari, E. & Scacco, U. First age and growth estimates in the deep-water shark, Etmopterus spinax (Linnaeus, 1758), by deep coned vertebral analysis. Mar. Biol. 152(5), 1207–1214, 10.1007/s00227-007-0769-y (2007). DOI: 10.1007/s00227-007-0769-y
Claes, J. M. & Mallefet, J. Early development of bioluminescence suggests camouflage by counter-illumination in the velvet belly lantern shark Etmopterus spinax (Squaloidea: Etmopteridae). J. Fish Biol. 73(6), 1337–1350, 10.1111/j.1095-8649.2008.02006.x (2008). DOI: 10.1111/j.1095-8649.2008.02006.x
Yano, K. & Musick, J. A. The effect of the mesoparasitic barnacle Anelasma on the development of reproductive organs of deep-sea squaloid sharks, Centroscyllium and Etmopterus. Environ. Biol. Fish 59(3), 329–339, 10.1023/A:1007649227422 (2000). DOI: 10.1023/A:1007649227422
Isbert, W. et al. Metazoan parasite communities and diet of the velvet belly lantern shark Etmopterus spinax (Squaliformes: Etmopteridae): a comparison of two deep-sea ecosystems. J. Fish Biol. 86(2), 687–706, 10.1111/jfb.12591 (2015). DOI: 10.1111/jfb.12591
Rees, D. J. et al. De novo innovation allows shark parasitism and global expansion of the barnacle Anelasma squalicola. Curr. Biol. 29(12), R562–R563, 10.1016/j.cub.2019.04.053 (2019). DOI: 10.1016/j.cub.2019.04.053
Carbonell, A., Alemany, F., Merella, P., Quetglas, A. & Roman, E. The by-catch of sharks in the western Mediterranean (Balearic Islands) trawl fishery. Fish. Res. 61, 7–18, 10.1016/S0165-7836(02)00242-4 (2003). DOI: 10.1016/S0165-7836(02)00242-4
Serena, F., Cecchi, E., Mancusi, C. & Pajetta, R. Contribution to the knowledge of the biology of Etmopterus spinax (Linnaeus, 1758)(Chondrichthyes, Etmopteridae). FAO Fisheries Proceedings 3, 388–394.
Renwart, M., Delroisse, J., Claes, J. M. & Mallefet, J. Ultrastructural organization of lantern shark (Etmopterus spinax Linnaeus, 1758) photophores. Zoomorphology 133(4), 405–416, 10.1007/s00435-014-0230-y (2014). DOI: 10.1007/s00435-014-0230-y
Renwart, M., Delroisse, J., Flammang, P., Claes, J. M. & Mallefet, J. Cytological changes during luminescence production in lanternshark (Etmopterus spinax Linnaeus, 1758) photophores. Zoomorphology. 134(1), 107–116, 10.1007/s00435-014-0235-6 (2015). DOI: 10.1007/s00435-014-0235-6
Duchatelet, L., Delroisse, J., Flammang, P., Mahillon, J. & Mallefet, J. Etmopterus spinax, the velvet belly lanternshark, does not use bacterial luminescence. Acta Histochem. 121, 516–521, 10.1016/j.acthis.2019.04.010 (2019). DOI: 10.1016/j.acthis.2019.04.010
Claes, J. M., Kronstrom, J., Holmgren, S. & Mallefet, J. Nitric oxide in the control of luminescence from lantern shark (Etmopterus spinax) photophores. J. Exp. Biol. 213(Pt 17), 3005–3011, 10.1242/jeb.040410 (2010). DOI: 10.1242/jeb.040410
Claes, J. M., Kronstrom, J., Holmgren, S. & Mallefet, J. GABA inhibition of luminescence from lantern shark (Etmopterus spinax) photophores. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 153(2), 231–236, 10.1016/j.cbpc.2010.11.002 (2011). DOI: 10.1016/j.cbpc.2010.11.002
Duchatelet, L., Delroisse, J., & Mallefet, J. Bioluminescence in lanternsharks: insight from hormone receptor localization. Gen. Comp. Endocrinol. 294, 113488, https://doi.org/10.1016/j.ygcen.2020.113488
Delroisse, J., Duchatelet, L., Flammang, P. & Mallefet, J. De novo transcriptome analyses provide insights into opsin-based photoreception in the lanternshark Etmopterus spinax. PLoS One. 13(12), e0209767, 10.1371/journal.pone.0209767 (2018). DOI: 10.1371/journal.pone.0209767
Duchatelet, L., Claes, J. M. & Mallefet, J. Embryonic expression of encephalopsin supports bioluminescence perception in lanternshark photophores. Mar. Biol. 166, 21, 10.1007/s00227-019-3473-9 (2019). DOI: 10.1007/s00227-019-3473-9
Tong, D. et al. Evidence for light perception in a bioluminescent organ. Proc. Natl. Acad. Sci. USA 106(24), 9836–9341, 10.1073/pnas.0904571106 (2009). DOI: 10.1073/pnas.0904571106
McFall-Ngai, M., Heath-Heckman, E. A. C., Gillette, A. A., Peyer, S. M. & Harvie, E. A. The secret languages of coevolved symbioses: Insights from the Euprymna scolopes-Vibrio fischeri symbiosis. Semin. Immunol. 24(1), 3–8, 10.1016/j.smim.2011.11.006 (2012). DOI: 10.1016/j.smim.2011.11.006
Schnitzler, C. E. et al. Genomic organization, evolution, and expression of photoprotein and opsin genes in Mnemiopsis leidyi: a new view of ctenophore photocytes. BMC Biology. 10, 107, 10.1186/1741-7007-10-107 (2012). DOI: 10.1186/1741-7007-10-107
Delroisse, J. et al. High opsin diversity in a non-visual infaunal brittle star. BMC Genomics. 15, 1035, 10.1186/1471-2164-15-1035 (2014). DOI: 10.1186/1471-2164-15-1035
Terakita, A. et al. Expression and comparative characterization of Gq-coupled invertebrate visual pigments and melanopsin. J. Neurochem. 105(3), 883–890, 10.1111/j.1471-4159.2007.05184.x (2008). DOI: 10.1111/j.1471-4159.2007.05184.x
Fujii, R., Wakatabi, H. & Oshima, N. Inositol 1,4,5-trisphosphate signals the motile response of fish chromatophores—I. Aggregation of pigment in the tilapia melanophore. J. Exp. Biol. 259(1), 9–17, 10.1002/jez.1402590103 (1991). DOI: 10.1002/jez.1402590103
Thaler, C. D. & Haimo, L. T. Regulation of organelle transport in melanophores by calcineurin. J. Cell Biol. 111(5), 1939–1948, 10.1083/jcb.111.5.1939 (1990). DOI: 10.1083/jcb.111.5.1939
Ingold, A. L., Cohn, S. A. & Scholey, J. M. Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains. J. Cell Biol. 107(6), 2657–2667, 10.1083/jcb.107.6.2657 (1988). DOI: 10.1083/jcb.107.6.2657
Tuma, M. C., Zill, A., Le Bot, N., Vernos, I. & Gelfand, V. I. Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores. J. Cell Biol. 143(6), 1547–1558, 10.1083/jcb.143.6.1547 (1998). DOI: 10.1083/jcb.143.6.1547
Sugihara, T., Nagata, T., Mason, B., Koyanagi, M. & Terakita, A. Absorption Characteristics of Vertebrate Non-Visual Opsin, Opn3. PloS One. 11(8), e0161215, 10.1371/journal.pone.0161215 (2016). DOI: 10.1371/journal.pone.0161215
Kato, M. et al. Two opsin 3-related proteins in the chicken retina and brain: a TMT-type opsin 3 is a blue-light sensor in retinal horizontal cells, hypothalamus, and cerebellum. PLoS One. 11(11), e0163925, 10.1371/journal.pone.0163925 (2016). DOI: 10.1371/journal.pone.0163925
Koyanagi, M., Takada, E., Nagata, T., Tsukamoto, H. & Terakita, A. Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue. Proc. Natl. Acad. Sci. USA 110(13), 4998–5003, 10.1073/pnas.1219416110 (2013). DOI: 10.1073/pnas.1219416110
Terakita, A. & Nagata, T. Functional properties of opsins and their contribution to light-sensing physiology. Zool. Sci. 31(10), 653–659, 10.2108/zs140094 (2014). DOI: 10.2108/zs140094
Nagata, T., Koyanagi, M., Lucas, R. & Terakita, A. An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor. Sci. Rep. 8(1), 3535, 10.1038/s41598-018-21946-1 (2018). DOI: 10.1038/s41598-018-21946-1
Abe, K. et al. Role of cyclic AMP in mediating the effects of MSH, norepinephrine, and melatonin on frog skin color. Endocrinol. 85(4), 674–682, 10.1210/endo-85-4-674 (1969). DOI: 10.1210/endo-85-4-674
White, B. H., Sekura, R. D. & Rollag, M. D. Pertussis toxin blocks melatonin-induced pigment aggregation in Xenopus dermal melanophores. J. Comp. Physiol. B 157(2), 153–159, 10.1007/BF00692359 (1987). DOI: 10.1007/BF00692359
Vanacek, J. Cellular mechanisms of melatonin action. Physiol. Rev. 78(3), 687–721, 10.1152/physrev.1998.78.3.687 (1998). DOI: 10.1152/physrev.1998.78.3.687
Sugden, D., Davidson, K. & Hough, K. A., The, M.-T. Melatonin. melatonin receptors and melanophores: a moving story. Pigment Cell Res. 17(5), 454–460, 10.1111/j.1600-0749.2004.00185.x (2004). DOI: 10.1111/j.1600-0749.2004.00185.x
Schmidt, C. J., Thomas, T. C. & Neer, E. J. Specificity of G protein beta and gamma subunit interactions. J. Biol. Chem. 267, 13807–13810 (1992).
Standifer, K. M. & Pasternak, G. W. G proteins and opioid receptor-mediated signalling. Cell. Signal. 9(3), 237–248, 10.1016/S0898-6568(96)00174-X (1997). DOI: 10.1016/S0898-6568(96)00174-X
Mullins, U. L., Fernandes, P. B. & Eison, A. S. Melatonin agonists induce phophoinositide hydrolysis in Xenopus laevis melanophores. Cell. Signal. 9(2), 169–173, 10.1016/S0898-6568(96)00137-4 (1997). DOI: 10.1016/S0898-6568(96)00137-4
Luby-Phelps, K. & Porter, K. R. The control of pigment migration in isolated erythrophores of holocentrus ascensionis (Osbeck). II. The role of calcium. Cell. 29(2), 441–450, 10.1016/0092-8674(82)90160-X (1982). DOI: 10.1016/0092-8674(82)90160-X
Fujii, R. & Oshima, N. Control of chromatophore movements in teleost fishes. Zool. Sci. 3, 13–47 (1986).
Oshima, N., Suzuki, M., Yamaji, N. & Fujii, R. Pigment aggregation is triggered by an increase in free calcium ions within fish chromatophores. Comp. Biochem. Physiol. A Physiol. 91(1), 27–32, 10.1016/0300-9629(88)91587-3 (1988). DOI: 10.1016/0300-9629(88)91587-3
Kotz, K. & McNiven, M. Intracellular calcium and cAMP regulate directional pigment movements in teleost erythrophores. J. Cell Biol. 124(4), 463–474, 10.1083/jcb.124.4.463 (1994). DOI: 10.1083/jcb.124.4.463
Phatarpekar, P. V. et al. Molecular and pharmacological characterization of muscarinic receptors in retinal pigment epithelium: role in light-adaptive pigment movements. J. Neurochem. 95(5), 1504–1520, 10.1111/j.1471-4159.2005.03512.x (2005). DOI: 10.1111/j.1471-4159.2005.03512.x
Johnson, A. S. & García, D. M. Carbachol-mediated pigment granule dispersion in retinal pigment epithelium requires Ca2+ and calcineurin. BMC Cell Biol. 8(1), 53, 10.1186/1471-2121-8-53 (2007). DOI: 10.1186/1471-2121-8-53
Oshima, N., Hayakawa, M. & Sugimoto, M. The involvement of calmodulin in motile activities of fish chromatophores. Comp. Biochem. Physiol. C Comp. Pharmacol. 97(1), 33–36, 10.1016/0742-8413(90)90167-8 (1990). DOI: 10.1016/0742-8413(90)90167-8
Nery, L. E. M., da Silva, M. A., Josefsson, L. & Castrucci, A. M. L. Cellular signalling of PCH-induced pigment aggregation in the crustacean Macrobrachium potiuna erythrophores. J. Comp. Physiol. 167(8), 570–575, 10.1007/s003600050111 (1997). DOI: 10.1007/s003600050111
Clark, T. G. & Rosenbaum, J. L. Pigment particle translocation in detergent-permeabilized melanophores of Fundulus heteroclitus. Proc. Natl. Acad. Sci. USA 79(15), 4655–4659, 10.1073/pnas.79.15.4655 (1982). DOI: 10.1073/pnas.79.15.4655
Nilsson, H., Rutberg, M. & Wallin, M. Localization of kinesin and cytoplasmic dynein in cultured melanophores from Atlantic cod, Gadus morhua. Cell Motil. Cytoskeleton. 33(3), 183–196, 10.1002/(SICI)1097-0169(1996)33:3<183::AID-CM3>3.0.CO;2-C (1996). DOI: 10.1002/(SICI)1097-0169(1996)33:3<183::AID-CM3>3.0.CO;2-C
Nilsson, H. & Wallin, M. Evidence for several roles of dynein in pigment transport in melanophores. Cell. Motil. Cytoskeleton. 38(4), 397–409, 10.1002/(SICI)1097-0169(1997)38:4<397::AID-CM9>3.0.CO;2-0 (1997). DOI: 10.1002/(SICI)1097-0169(1997)38:4<397::AID-CM9>3.0.CO;2-0
McClintock, T. S., Rising, J. P. & Lerner, M. R. Melanophore pigment dispersion responses to agonists show two patterns of sensitivity to inhibitors of cAMP-dependent protein kinase and protein kinase C. J. Cell Physiol. 167(1), 1–7, 10.1002/(SICI)1097-4652(199604)167:1<1::AID-JCP1>3.0.CO;2-T (1996). DOI: 10.1002/(SICI)1097-4652(199604)167:1<1::AID-JCP1>3.0.CO;2-T
Reilein, A. R., Tint, I. S., Peunova, N. I., Enikolopov, G. N. & Gelfand, V. I. Regulation of organelle movement in melanophores by protein kinase A (PKA), protein kinase C (PKC), and protein phosphatase 2A (PP2A). J. Cell Biol. 142(3), 803–813, 10.1083/jcb.142.3.803 (1998). DOI: 10.1083/jcb.142.3.803
Rodionov, V., Yi, J., Kashina, A., Oladipo, A. & Gross, S. P. Switching between microtubule- and actin-based transport systems in melanophores is controlled by cAMP levels. Curr. Biol. 13(21), 1837–1847, 10.1016/j.cub.2003.10.027 (2003). DOI: 10.1016/j.cub.2003.10.027
de Graan, P. N. E., Oestreicher, A. B., Zwiers, H., Gispen, W. H. & van de Veerdonk, F. C. G. Characterization of α-MSH-induced changes in the phosphorylation of a 53 kDa protein in Xenopus melanophores. Mol. Cell. Endocrinol. 42(2), 127–133, 10.1016/0303-7207(85)90100-5 (1985). DOI: 10.1016/0303-7207(85)90100-5
Reilein, A. R. et al. Differential regulation of dynein-driven melanosome movement. Biochem. Biophys. Res. Commun. 309(3), 652–658, 10.1016/j.bbrc.2003.08.047 (2003). DOI: 10.1016/j.bbrc.2003.08.047
Hadley, M. E. Calcium-Dependent Irreversible Effect of Ionophore A23187 on Melanophores. Pigment Cell Melanoma Res. 1(1), 57–61, 10.1111/j.1600-0749.1987.tb00535.x (1987). DOI: 10.1111/j.1600-0749.1987.tb00535.x
Jones, B. W. & Nishigichi, M. K. Counterillumination in the Hawaiian bobtail squid, Euprymna scolopes Berry (Mollusca: Cephalopoda). Mar. Biol. 144, 1151–1155, 10.1007/s00227-003-1285-3 (2004). DOI: 10.1007/s00227-003-1285-3
Young, R. E. & Mencher, F. M. Bioluminescence in mesopelagic squid: diel color change during counterillumination. Science. 208(4449), 1286–1288, 10.1126/science.208.4449.1286 (1980). DOI: 10.1126/science.208.4449.1286
Harper, R. D. & Case, J. F. Disruptive counterillumination and its anti-predatory value in the plainfish midshipman Prichthys notatus. Mar. Biol. 134, 529–540, 10.1007/s002270050568 (1999). DOI: 10.1007/s002270050568
Hastings, J. W. Light to hide by: ventral luminescence to camouflage the silhouette. Science. 173(4001), 1016–1017, 10.1126/science.173.4001.1016 (1971). DOI: 10.1126/science.173.4001.1016
Duchatelet, L., Oury, N., Mallefet, J. & Magalon, H. In the intimacy of the darkness: genetic polyandry in deep-sea luminescent lanternsharks Etmopterus spinax and Etmopterus molleri (Squaliformes, Etmopteridae). J. Fish Biol. 2020, 1–7, 10.1111/jfb.14336 (2020). DOI: 10.1111/jfb.14336
Bernald, D., Donley, J. M., Shadwick, R. E. & Syme, D. A. Mammal-like muscles power swimming in a cold water shark. Nature. 437(7063), 1349–1352, 10.1038/nature04007 (2005). DOI: 10.1038/nature04007
Sun, L. et al. Distribution of mammalian-like melanopsin in cyclostome retinas exhibiting a different extent of visual functions. PLoS One. 9(9), e108209, 10.1371/journal.pone.0108209 (2014). DOI: 10.1371/journal.pone.0108209
Molday, R. S. & MacKenzie, D. Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes. Biochemistry. 22(3), 653–660, 10.1021/bi00272a020 (1983). DOI: 10.1021/bi00272a020
Koyanagi, M. et al. pigment in the lamprey pineal. Proc. Natl. Acad. Sci. USA 101(17), 6687–6691, 10.1073/pnas.0400819101 (2004). DOI: 10.1073/pnas.0400819101
Tsukamoto, H. & Farrens, D. L. A constitutively activating mutation alters the dynamics and energentics of a key conformational change in a ligand-free G protein-coupled receptor. J. Biol. Chem. 288(39), 28207–28216, 10.1074/jbc.M113.472464 (2013). DOI: 10.1074/jbc.M113.472464
Firestone, A. J. et al. Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein. Nature. 484, 125, 10.1038/nature10936 (2012). DOI: 10.1038/nature10936
