Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor–interacting protein–like 1 with the regulatory P$γ$ subunit of phosphodiesterase 6

Yadav, Ravi P.; Boyd, Kimberly; Yu, Liping; Artemyev, Nikolai O.

doi:10.1074/jbc.RA119.010666

Title: Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor–interacting protein–like 1 with the regulatory P$$γ$$ subunit of phosphodiesterase 6

Journal Article · Thu Sep 05 00:00:00 EDT 2019 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.RA119.010666· OSTI ID:1599440

Yadav, Ravi P. ^[1]; Boyd, Kimberly ^[1]; Yu, Liping ^[1];

^[1]

Univ. of Iowa, Iowa City, IA (United States). Carver College of Medicine

Phosphodiesterase-6 (PDE6) is key to both phototransduction and health of rods and cones. Proper folding of PDE6 relies on the chaperone activity of aryl hydrocarbon receptor–interacting protein–like 1 (AIPL1), and mutations in both PDE6 and AIPL1 can cause a severe form of blindness. Although AIPL1 and PDE6 are known to interact via the FK506-binding protein domain of AIPL1, the contribution of the tetratricopeptide repeat (TPR) domain of AIPL1 to its chaperone function is poorly understood. In this work, we demonstrate that AIPL1–TPR interacts specifically with the regulatory P$$γ$$ subunit of PDE6. Use of NMR chemical shift perturbation (CSP) mapping technique revealed the interface between the C-terminal portion of P$$γ$$ and AIPL1–TPR. Our solution of the crystal structure of the AIPL1–TPR domain provided additional information, which together with the CSP data enabled us to generate a model of this interface. Biochemical analysis of chimeric AIPL1–AIP proteins supported this model and also revealed a correlation between the affinity of AIPL1–TPR for P$$γ$$ and the ability of P$$γ$$ to potentiate the chaperone activity of AIPL1. Based on these results, we present a model of the larger AIPL1–PDE6 complex. This supports the importance of simultaneous interactions of AIPL1–FK506–binding protein with the prenyl moieties of PDE6 and AIPL1–TPR with the P$$γ$$ subunit during the folding and/or assembly of PDE6. This study sheds new light on the versatility of TPR domains in protein folding by describing a novel TPR-protein binding partner, P$$γ$$, and revealing that this subunit imparts AIPL1 selectivity for its client.

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Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

Sponsoring Organization:: USDOE Office of Science (SC); National Institute of General Medical Sciences (NIGMS); National Institutes of Health (NIH); Knights Templar Eye Foundation

Grant/Contract Number:: AC02-05CH11231; AC02-06CH11357; 9 P41 GM103622; 1S10OD018090-01; RO1 EY-10843; 18384800

OSTI ID:: 1599440

Journal Information:: Journal of Biological Chemistry, Vol. 294, Issue 43; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Title: Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor–interacting protein–like 1 with the regulatory P$$γ$$ subunit of phosphodiesterase 6

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