NDLI: Role of the conserved NPxxY(x)5,6F motif in the rhodopsin ground state and during activation

Content Provider	PubMed Central
Author	Fritze, Olaf Filipek, Sławomir Kuksa, Vladimir Palczewski, Krzysztof Hofmann, Klaus Peter Ernst, Oliver P.
Copyright Year	2003
Abstract	In the G protein-coupled receptor rhodopsin, the conserved NPxxY(x)5,6F motif connects the transmembrane helix VII and the cytoplasmic helix 8. The less geometrically constrained retinal analogue 9-demethyl-retinal prevents efficient transformation of rhodopsin to signaling metarhodopsin (Meta) II after retinal photoisomerization. Here, we demonstrate that Ala replacement mutations within the NPxxY(x)5,6F domain, which eliminate an interaction between aromatic residues Y306 and F313, allow formation of Meta II despite the presence of 9-demethyl-retinal. Also a disulfide bond linking residues 306 and 313 in the 9-demethyl-retinal-reconstituted mutant Y306C/F313C/C316S prevented Meta II formation, whereas the reduced form of the mutant readily transformed to Meta II after illumination. These observations suggest that the interaction between residues 306 and 313 is disrupted during the Meta I/Meta II transition. However, this enhancement in Meta II formation is not reflected in the G protein activation, which is dramatically reduced for these mutants, suggesting that changes in the Y306–F313 interaction also lead to a proper realigning of helix 8 after photoisomerization. The E134Q mutation, located in the second conserved motif, D(E)RY, rescues activity in 9-demethyl-retinal-reconstituted mutants to different degrees, depending on the position of the Ala replacement in the NPxxY(x)5,6F motif, thus revealing distinct roles for the NP and Y(x)5,6F portions. Our studies underscore the importance of the NPxxY(x)5,6F and D(E)RY motifs in providing structural constraints in rhodopsin that rearrange in response to photoisomerization during formation of the G protein-activating Meta II. The dual control of the structural rearrangements secures reliable transformation of quiescent rhodopsin to activating Meta II.
Related Links	http://dx.doi.org/10.1073/pnas.0435715100
Ending Page	2295
Page Count	6
Starting Page	2290
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	100
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2003-03-04
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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