First published December 1, 2014 - More info
The osteoblast-derived hormone osteocalcin promotes testosterone biosynthesis in the mouse testis by binding to GPRC6A in Leydig cells. Interestingly,
Franck Oury, Mathieu Ferron, Wang Huizhen, Cyrille Confavreux, Lin Xu, Julie Lacombe, Prashanth Srinivas, Alexandre Chamouni, Francesca Lugani, Herve Lejeune, T. Rajendra Kumar, Ingrid Plotton, Gerard Karsenty
Original citation: J Clin Invest. 2013;123(6):2421–2433. doi:10.1172/JCI65952.
Citation for this corrigendum: J Clin Invest. 2014;124(12):5522. doi:10.1172/JCI79293.
In the original article, the substitution mutation in GPRC6A at F464Y was erroneously described as located in one of the transmembrane domains of GPRC6A; however, the F464Y mutation is located in the long N-terminal region of GPRC6A (1-594AA). This error affected portions of the text in the Abstract, Introduction, Results, and Discussion. The corrected sentences appear below.
Abstract (page 2421):
To determine the importance of osteocalcin in humans, we analyzed a cohort of patients with primary testicular failure and identified 2 individuals harboring the same heterozygous missense variant of GPRC6A, which prevented the receptor from localizing to the cell membrane.
Introduction (page 2421):
In trying to expand the biological relevance of osteocalcin from mouse to human, we identified in 2 patients with peripheral testicular failure the same amino acid substitution affecting a highly conserved residue in the long N-terminal domain (1-594AA) of GPRC6A.
Results (page 2429):
We sequenced all exons of Osteocalcin and GPRC6A, the receptor mediating osteocalcin reproductive function in Leydig cells (2), in these patients. Two patients in this cohort harbored a T→A transversion in exon 4 (g.117121904A/T), resulting in an amino acid substitution in the long N-terminal domain of GPRC6A (F464Y) (Figure 7, A and B, and Supplemental Figure 6A).
Discussion (page 2431):
This missense mutation affected a highly conserved residue, occurred in the N-terminal domain region of the molecule, and prevented its localization to the cell membrane, therefore resulting in a loss of function of GPRC6A.
The authors regret the error.