Fic蛋白家族的研究进展

过去的研究发现了一个具有相同保守结构域的Fic(filamentation induced by cAMP)蛋白家族。虽然在原核生物中发现超过3 000种以上含有Fic结构域的不同蛋白质,但到目前为止,在包括人在内的真核生物中仅发现一种Fic蛋白。Fic结构域主要通过含有磷酸基团的化合物在转录中起作用,目前被人类关注的功能是单酰磷酸化(AMPylation, AMP化),一种类似磷酸化的蛋白质调控机制,是以ATP为底物将一磷酸腺苷(AMP)特异地转移至靶标氨基酸残基。该机制主要在细菌侵袭宿主、侵袭后增殖、致病的过程中发挥作用。真核细胞中的单磷酸腺苷化可以调控内质网的稳定性。本文主要对Fic蛋白的特征性结构和作用以及几种主要的Fic蛋白的结构、作用和研究方法进行综述。

Progress in research on Fic protein family

In the past research progress, a protein family has been found with the same conserved domain called Fic(filamentation induced by cAMP). More than 3 000 different proteins containing Fic domains have been found in prokaryotes. So far, only one Fic protein has been found in eukaryotes including humans. The Fic domain mainly plays a role in post-translational modification by a compound containing a phosphate group. Currently, the function of human attention is AMPylation, a phosphorylation-like protein regulation mechanism, with ATP as the substrate specifically transfers AMP to the target amino acid residue. This mechanism mainly plays a role in bacterial invasion of the host, proliferation after invasion, and pathogenesis. AMPylation in eukaryotic cells can regulate the stability of the endoplasmic reticulum. This paper mainly describes the characteristic structure and function of Fic protein, as well as the structure, function and research methods of several major Fic proteins.