ArticleProceedings of the National Academy of Sciences of the United States of America2001
J3-crystallin of the jellyfish lens: similarity to saposins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 50 citations in OpenAlex.
- Contributions of aquatic organisms to understanding the vertebrate ocular lens.Frontiers in ophthalmology · 2026Review
- Comparative analysis of the structure and crystallin composition of the lenses of freshwater fish and gastropods with respect to their vision.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2025Article
- Light modulated cnidocyte discharge predates the origins of eyes in Cnidaria.Ecology and evolution · 2021Article
- Characterization of secondary structure and lipid binding behavior of N-terminal saposin like subdomain of human Wnt3a.Archives of biochemistry and biophysics · 2017Article
- The cuticular nature of corneal lenses in Drosophila melanogaster.Development genes and evolution · 2017Article
- A new transcriptome and transcriptome profiling of adult and larval tissue in the box jellyfish Alatina alata: an emerging model for studying venom, vision and sex.BMC genomics · 2016Article
- The molecular refractive function of lens γ-Crystallins.Journal of molecular biology · 2011Article
- Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm.PloS one · 2011Article
- Evolution of graded refractive index in squid lenses.Journal of the Royal Society, Interface · 2007Article
- Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A short guided tour through functional and structural features of saposin-like proteins.The Biochemical journal · 2005Review
- Vertebrate-like betagamma-crystallins in the ocular lenses of a copepod.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2005Article
- Crystallin genes: specialization by changes in gene regulation may precede gene duplication.Journal of structural and functional genomics · 2003Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
J3-crystallin, one of the three major eye-lens proteins of the cubomedusan jellyfish (Tripedalia cystophora), shows similarity to vertebrate saposins, which are multifunctional proteins that bridge lysosomal hydrolases to lipids and activate enzyme activity. Sequence alignment of deduced J3-crystallin indicates two saposin-like motifs arranged in tandem, each containing six cysteines characteristic of this protein family. The J3-crystallin cDNA encodes a putative precursor analogous to vertebrate prosaposins. The J3-crystallin gene has seven exons, with exons 2-4 encoding the protein. Exon 3 encodes a circularly permutated saposin motif, called a swaposin, found in plant aspartic proteases. J3-crystallin RNA was found in the cubomedusan lens, statocyst, in bands radiating from the pigmented region of the ocellus, in the tentacle tip by in situ hybridization, and in the embryo and larva by reverse transcription-PCR. Our data suggest a crystallin role for the multifunctional saposin protein family in the jellyfish lens. This finding extends the gene sharing evolutionary strategy for lens crystallins to the cnidarians and indicates that the putative primordial saposin/swaposin J3-crystallin reflects both the chaperone and enzyme connections of the vertebrate crystallins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.