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Retinylidene proteins: structures and functions from archaea to humans
J L Spudich1, C S Yang, K H Jung
1Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030, USA. spudich@utmmg.med.uth.tmc.edu
Annual Review of Cell and Developmental Biology
|October 14, 2000
Summary
Retinylidene proteins are found across life, from microbes to humans, performing vital light-sensing functions. This review explores their diverse structures and functions in photoreception and signaling.
Area of Science:
- Biochemistry
- Molecular Biology
- Photobiology
Background:
- Retinylidene proteins are seven-membrane-spanning proteins binding the chromophore retinal.
- These proteins are present in diverse organisms, including prokaryotes, eukaryotes, and animals.
- They play roles in light-driven ion transport, phototaxis, and photosignal transduction.
Purpose of the Study:
- To review retinylidene proteins as a group.
- To summarize structure-function relationships in well-studied examples.
- To report recent advancements in the field.
Main Methods:
- Literature review of existing research on retinylidene proteins.
- Analysis of structure-function data from various organisms.
- Synthesis of recent findings and developments.
Main Results:
- Ubiquitous distribution of retinylidene proteins across diverse life forms.
- Varied functions including ion transport, signaling, and isomerization.
- Established structure-function correlations in key examples.
Conclusions:
- Retinylidene proteins represent a conserved yet functionally diverse protein family.
- Understanding their structure is key to elucidating their varied biological roles.
- Ongoing research continues to uncover new functions and mechanisms.