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Cell Signal. 2017 Dec;40:183-189. doi: 10.1016/j.cellsig.2017.09.014. Epub 2017 Sep 20.

AIPL1: A specialized chaperone for the phototransduction effector.

Author information

1
Department of Molecular Physiology and Biophysics, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, United States.
2
Department of Molecular Physiology and Biophysics, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, United States; Department of Ophthalmology and Visual Sciences, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, United States. Electronic address: nikolai-artemyev@uiowa.edu.

Abstract

Molecular chaperones play pivotal roles in protein folding, quality control, assembly of multimeric protein complexes, protein trafficking, stress responses, and other essential cellular processes. Retinal photoreceptor rod and cone cells have an unusually high demand for production, quality control, and trafficking of key phototransduction components, and thus, require a robust and specialized chaperone machinery to ensure the fidelity of sensing and transmission of visual signals. Misfolding and/or mistrafficking of photoreceptor proteins are known causes for debilitating blinding diseases. Phosphodiesterase 6, the effector enzyme of the phototransduction cascade, relies on a unique chaperone aryl hydrocarbon receptor (AhR)-interacting protein-like 1 (AIPL1) for its stability and function. The structure of AIPL1 and its relationship with the client remained obscure until recently. This review summarizes important recent advances in understanding the mechanisms underlying normal function of AIPL1 and the protein perturbations caused by pathogenic mutations.

KEYWORDS:

AIPL1; FKBP domain; Molecular chaperone; Phosphodiesterase 6; Photoreceptor; Retina

PMID:
28939106
PMCID:
PMC6022367
DOI:
10.1016/j.cellsig.2017.09.014
[Indexed for MEDLINE]
Free PMC Article

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