The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban

ABSTRACT: Signal peptide peptidase (SPP) and the four homologous SPP-like (SPPL) proteases constitute a family of intramembrane aspartyl proteases with selectivity for type II-oriented transmembrane segments. Here, we analyse the physiological function of the orphan protease SPPL2c, previously considered to represent a non-expressed pseudogene. We demonstrate proteolytic activity of SPPL2c towards selected tail-anchored proteins. Despite shared ER localization, SPPL2c and SPP exhibit distinct, though partially overlapping substrate spectra and inhibitory profiles, and are organised in different high molecular-weight complexes. Interestingly, SPPL2c is specifically expressed in murine and human testis where it is primarily localised in spermatids. In mice, SPPL2c-deficiency leads to a partial loss of

SUBMITTER: Mr. Johannes Niemeyer 

PROVIDER: S-SCDT-EMBOR-2018-46449-T | biostudies-other |

REPOSITORIES: biostudies-other