TY - JOUR
T1 - Pinopsin evolved as the ancestral dim-light visual opsin in vertebrates
AU - Sato, Keita
AU - Yamashita, Takahiro
AU - Kojima, Keiichi
AU - Sakai, Kazumi
AU - Matsutani, Yuki
AU - Yanagawa, Masataka
AU - Yamano, Yumiko
AU - Wada, Akimori
AU - Iwabe, Naoyuki
AU - Ohuchi, Hideyo
AU - Shichida, Yoshinori
N1 - Funding Information:
We thank Prof. R.S. Molday for the generous gift of a Rho1D4-producing hybridoma, Prof. J. Nathans for providing the HEK293S cell line, Prof. H. Niwa for pCAGGS vector, Prof. K. Nishikawa for the tissues of R. catesbeiana, and The Institute for Amphibian Biology (Hiroshima University, Hiroshima, Japan) for X. tropicalis through the National Bio-Resource Project of the Ministry of Education, Culture, Sports, Science, and Technology of Japan (MEXT). This work was supported in part by Grants-in Aid for Scientific Research of MEXT to K. Sato (17K15159), T.Y. (15H00812, 16K07437), and Y.S. (26650119, 16H02515), a grant from the Takeda Science Foundation (T.Y.), Grant for Basic Science Research Projects from The Sumitomo Foundation (T.Y.), and CREST, JST JPMJCR1753 (to T.Y.).
Publisher Copyright:
© 2018, The Author(s).
PY - 2018/12/1
Y1 - 2018/12/1
N2 - Pinopsin is the opsin most closely related to vertebrate visual pigments on the phylogenetic tree. This opsin has been discovered among many vertebrates, except mammals and teleosts, and was thought to exclusively function in their brain for extraocular photoreception. Here, we show the possibility that pinopsin also contributes to scotopic vision in some vertebrate species. Pinopsin is distributed in the retina of non-teleost fishes and frogs, especially in their rod photoreceptor cells, in addition to their brain. Moreover, the retinal chromophore of pinopsin exhibits a thermal isomerization rate considerably lower than those of cone visual pigments, but comparable to that of rhodopsin. Therefore, pinopsin can function as a rhodopsin-like visual pigment in the retinas of these lower vertebrates. Since pinopsin diversified before the branching of rhodopsin on the phylogenetic tree, two-step adaptation to scotopic vision would have occurred through the independent acquisition of pinopsin and rhodopsin by the vertebrate lineage.
AB - Pinopsin is the opsin most closely related to vertebrate visual pigments on the phylogenetic tree. This opsin has been discovered among many vertebrates, except mammals and teleosts, and was thought to exclusively function in their brain for extraocular photoreception. Here, we show the possibility that pinopsin also contributes to scotopic vision in some vertebrate species. Pinopsin is distributed in the retina of non-teleost fishes and frogs, especially in their rod photoreceptor cells, in addition to their brain. Moreover, the retinal chromophore of pinopsin exhibits a thermal isomerization rate considerably lower than those of cone visual pigments, but comparable to that of rhodopsin. Therefore, pinopsin can function as a rhodopsin-like visual pigment in the retinas of these lower vertebrates. Since pinopsin diversified before the branching of rhodopsin on the phylogenetic tree, two-step adaptation to scotopic vision would have occurred through the independent acquisition of pinopsin and rhodopsin by the vertebrate lineage.
UR - http://www.scopus.com/inward/record.url?scp=85069668907&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85069668907&partnerID=8YFLogxK
U2 - 10.1038/s42003-018-0164-x
DO - 10.1038/s42003-018-0164-x
M3 - Article
C2 - 30302400
AN - SCOPUS:85069668907
VL - 1
JO - Communications Biology
JF - Communications Biology
SN - 2399-3642
IS - 1
M1 - 156
ER -