Olfactory marker protein interacts with adenosine nucleotide derivatives

Noriyuki Nakashima; Kie Nakashima; Akiko Nakashima; Makoto Takano

doi:10.1016/j.bbrep.2020.100887

Olfactory marker protein interacts with adenosine nucleotide derivatives

Biochem Biophys Rep. 2021 Jan 12:25:100887. doi: 10.1016/j.bbrep.2020.100887. eCollection 2021 Mar.

Authors

Noriyuki Nakashima¹, Kie Nakashima², Akiko Nakashima¹, Makoto Takano¹

Affiliations

¹ Department of Physiology, Kurume University School of Medicine, 67 Asahi-machi, Kurume, Fukuoka, 830-0011, Japan.
² Laboratory of Developmental Neurobiology, Graduate School of Biostudies, Kyoto University, Yoshida Hon-machi, Kyoto, 606-8501, Japan.

Abstract

Olfactory marker protein (OMP) is a genetic signature for mature olfactory receptor neurons (ORNs). Recently, it has been proposed that OMP directly captures odour-induced cAMP to swiftly terminate the olfactory signal transduction to maintain neuronal sensitivity. In the present study, we show that OMP can also interact with other adenosine nucleotides as ATP, ADP and AMP with different affinities. We performed bioluminescent resonant energy transfer (BRET) assay to measure the binding actions of the adenosine nucleotide derivatives in competition to cAMP. Amongst all, ATP showed the bell-shape affinity to OMP in the presence of cAMP; ADP and AMP showed fewer affinities to OMP than ATP. In the absence of cAMP analogues, ATP alone bound to OMP in a dose dependent manner with a lower affinity than to cAMP. Thus, OMP possessed different affinities to ATP in the presence or absence of cAMP. OMP may interact differentially with ATP and cAMP depending on its supply and demand along the cAMP-associated signalling in the limited spaces of cilia of ORNs.

Keywords: Adenosine nucleotide derivatives; Bioluminescent resonant energy transfer; Olfactory marker protein; cAMP-binding protein.