Journal article
AIPL1: A specialized chaperone for the phototransduction effector
Cellular signalling, Vol.40, pp.183-189
12/2017
DOI: 10.1016/j.cellsig.2017.09.014
PMCID: PMC6022367
PMID: 28939106
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.
•We summarize the accumulated evidence that AIPL1 is a specialized chaperone of PDE6.•We review recent structural advances in understanding the chaperone mechanisms of AIPL1.•We discuss unique protein dynamics of AIPL1 that are essential to its function.
Details
- Title: Subtitle
- AIPL1: A specialized chaperone for the phototransduction effector
- Creators
- Ravi P Yadav - Department of Molecular Physiology and Biophysics, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, United StatesNikolai O Artemyev - Department of Molecular Physiology and Biophysics, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, United States
- Resource Type
- Journal article
- Publication Details
- Cellular signalling, Vol.40, pp.183-189
- DOI
- 10.1016/j.cellsig.2017.09.014
- PMID
- 28939106
- PMCID
- PMC6022367
- NLM abbreviation
- Cell Signal
- ISSN
- 0898-6568
- eISSN
- 1873-3913
- Publisher
- Elsevier Inc
- Grant note
- DOI: 10.13039/100000002, name: National Institutes of Health, award: EY-10843, EY-12682
- Language
- English
- Date published
- 12/2017
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
- Record Identifier
- 9984025312402771
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