| Original language | English (US) |
|---|---|
| Pages (from-to) | 291-309 |
| Number of pages | 19 |
| Journal | Methods in Enzymology |
| Volume | 316 |
| DOIs | |
| State | Published - 2000 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
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Cultured amphibian melanophores : A model system to study melanopsin photobiology. / Rollag, Mark D.; Provencio, Ignacio; Sugden, David; Green, Carla B.
In: Methods in Enzymology, Vol. 316, 2000, p. 291-309.Research output: Contribution to journal › Review article › peer-review
}
TY - JOUR
T1 - Cultured amphibian melanophores
T2 - A model system to study melanopsin photobiology
AU - Rollag, Mark D.
AU - Provencio, Ignacio
AU - Sugden, David
AU - Green, Carla B.
N1 - Funding Information: Data currently available support the hypothesis that the photoactivated melanophore photopigment is coupled to adenylate cyclase through a Gs intermediate for melanosome dispersion and a Gi intermediate for photoag-gregation. Accordingly, during photodispersion of melanosomes, increased intracellular cAMP concentrations would activate cAMP-dependent protein kinase, which in turn would phosphorylate kinesin II s to cause melanosome dispersion. Decreased kinase activity in the face of constant protein phosphatase activity9 would result in a return of the melanosomes to an aggregated state. This hypothesis is supported by several observations. When photosensitive melanophores are exposed to light there is an increase in intracellular cAMP concentrations correlated with photodispersion of melanosomes2; cGMP does not mimic the effects of light, l° Inhibitors of cAMP-dependent protein kinase block the effect of light, but inhibitors of protein kinase C do not. 11 In the tailfin melanophores, the photoaggregation response is inhibited by pertussis toxin treatment, 12 consistent with coupling to Gi. Tailfin melanophores do not photoaggregate their melanosomes when intracellular cAMP is artificially clamped at high concentrations, but photoaggregate melanosomes normally when cGMP concentrations are pharmacologically manipulated. 12 Funding Information: We thank Mr. Atsushi Nakamura and Dr. Daisuke Kojima (in our laboratory) for technical assistance in overexpression of pinopsin, Dr. Fumio Tokunaga (at Osaka University) for providing expression vector pUSRa, and Dr. Jeremy Nathans (at Johns Hopkins University) for the kind gifts of pRSV-Tag and 293S cells. This work was supported in part by Grants-in-Aid from the Japanese Ministry of Education, Science, Sports, and Culture.
PY - 2000
Y1 - 2000
UR - http://www.scopus.com/inward/record.url?scp=0034012436&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034012436&partnerID=8YFLogxK
U2 - 10.1016/s0076-6879(00)16730-8
DO - 10.1016/s0076-6879(00)16730-8
M3 - Review article
C2 - 10800682
AN - SCOPUS:0034012436
VL - 316
SP - 291
EP - 309
JO - Methods in Enzymology
JF - Methods in Enzymology
SN - 0076-6879
ER -