The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins

doi:10.1016/0092-8674(91)90156-S

Cell

Volume 65, Issue 2, 19 April 1991, Pages 219-227

https://doi.org/10.1016/0092-8674(91)90156-S Get rights and content

Abstract

Mutations in the Drosophila ninaA gene cause dramatic reductions in rhodopsin levels, leading to Impaired visual function. The ninaA protein is a homolog of peptidyl-prolyl cis-trans isomerases. We find that ninaA is unique among this family of proteins in that it is an integral membrane protein, and it is expressed in a cell type-specific manner. We have used transgenic animals misexpressing different rhodopsins in the major class of photoreceptor cells to demonstrate that ninaA is required for normal function by two homologous rhodopsins, but not by a less conserved member of the Drosophila rhodopsin gene family. This demonstrates in vivo substrate specificity in a cyclophilin-like molecule. We also show that vertebrate retina contains a ninaA-related protein and that ninaA is a member of a gene family in Drosophila. These data offer insights into the in vivo role of this important family of proteins.

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^★: Present address: Department of Biology, San Diego State University, San Diego, California 92182

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Cell

ArticleThe cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins

Abstract

J. Biol. Chem.

J. Biol. Chem.

Cell

Cell

J. Biol. Chem.

Cell

Cell

Cell

Cell

Neuron

Cell

Biochem. Pharmacol.

J. Mol. Biol.

Immunol. Today

Cell

Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin

Probing immunosuppressant action with a nonnatural immunophilin ligand

Science

p1B15: a cDNA clone of the rat mRNA encoding cyclophilin

DNA

A point mutation of the rhodopsin gene in one form of retinitis pigmentosa

Nature

Cyclosporin A specifically inhibits function of nuclear proteins involved in T cell activation

Science

Targeted misexpression of a Drosophila opsin gene leads to altered visual function

Nature

Nachweis einer Enzymkatalyse für die cis-trans-Isomerisierung der Peptidbindung in prolinhaltigen Peptiden

Biomed. Biochim. Acta

Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

Nature

Etude optique in vivo des elements photoreceptors dans I'oeil compose de Drosophila

Kybernetik

Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

J. Cell Biol.

Complementary DNA for human T-cell cyclophilin

EMBO J.

Cyclophilin: a specific cytosolic binding protein for cyclosporin A

Science

A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

Nature

Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK506 binding protein: evidence for the existence of a family of distinct enzymes

Biochemistry

Transduction in invertebrate photoreceptors: role of pigment bi-stability

Physiol. Rev.

Article
The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins