Melatonin Target Proteins: Too Many or Not Enough?

Lei Liu; Nedjma Labani; Erika Cecon; Ralf Jockers

doi:10.3389/fendo.2019.00791

Melatonin Target Proteins: Too Many or Not Enough?

Front Endocrinol (Lausanne). 2019 Nov 15:10:791. doi: 10.3389/fendo.2019.00791. eCollection 2019.

Authors

Lei Liu^{1

2}, Nedjma Labani^{1

2}, Erika Cecon², Ralf Jockers²

Affiliations

¹ Cellular Signaling Laboratory, International Research Center for Sensory Biology and Technology of MOST, Key Laboratory of Molecular Biophysics of Ministry of Education, School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
² Université de Paris, Institut Cochin, CNRS, INSERM, Paris, France.

Abstract

The neurohormone N-acetyl-5-methoxytryptamine, better known as melatonin, is a tryptophan derivative with a wide range of biological effects that is present in many organisms. These effects are believed to rely either on the chemical properties of melatonin itself as scavenger of free radicals or on the binding of melatonin to protein targets. More than 15 proteins, including receptors (MT₁, MT₂, Mel1c, CAND2, ROR, VDR), enzymes (QR2, MMP-9, pepsin, PP2A, PR-10 proteins), pores (mtPTP), transporters (PEPT1/2, Glut1), and other proteins (HBS, CaM, tubulin, calreticuline), have been suggested to interact with melatonin at sub-nanomolar to millimolar melatonin concentrations. In this review we assemble for the first time the available information on proposed melatonin targets and discuss them in a comprehensive manner to evaluate the robustness of these findings in terms of methodology, physiological relevance, and independent replication.

Keywords: GPCR; Glut1; MMP-9; PEPT1/2; PR-10; QR2; ROR; melatonin.

Publication types

Review