Reimers Kerstin, Choi Claudia Y-U, Mau-Thek Eddy, Vogt Peter M
Klinik für Plastische, Hand- und Wiederherstellungschirurgie, Medizinische Hochschule Hannover, D-30659 Hannover, Germany.
Int J Mol Med. 2006 Oct;18(4):729-34.
Cellular sensitivity to apoptotic stimuli is determined by several regulatory proteins. The biological and biomedical impact of these regulatory proteins is of fundamental importance for understanding and controlling apoptotic processes. We used a bioinformatic approach to characterise the antiapoptotic protein Lifeguard (LFG). LFG is an evolutionarily well-conserved protein with homologues in many species. Due to its hydrophobic nature it is predicted to reside in cellular membranes, namely the endoplasmatic reticulum and the plasma membrane, with seven transmembrane spanners and a small cytoplasmic domain. The consensus motif of a protein family with unknown function UPF0005 was found in the C-terminus. The structure of Lifeguard resembles the antiapoptotic protein Bax Inhibitor-1 (BI-1). Concordantly, it was shown that Bax co-immunoprecipitates with LFG. Our results indicate that LFG belongs to a new cytoprotective family with evolutionarily conserved functions in the prevention of programmed cell death.
细胞对凋亡刺激的敏感性由多种调节蛋白决定。这些调节蛋白的生物学和生物医学影响对于理解和控制凋亡过程至关重要。我们采用生物信息学方法对抗凋亡蛋白救生员（LFG）进行了表征。LFG是一种在进化上高度保守的蛋白，在许多物种中都有同源物。由于其疏水性，预计它定位于细胞膜，即内质网和质膜，具有七个跨膜结构域和一个小的胞质结构域。在其C末端发现了一个功能未知的UPF0005蛋白家族的共有基序。救生员的结构类似于抗凋亡蛋白Bax抑制剂-1（BI-1）。与此一致的是，已表明Bax与LFG共免疫沉淀。我们的结果表明，LFG属于一个新的细胞保护家族，在预防程序性细胞死亡方面具有进化上保守的功能。
