Lydan M A, O'Day D H
Department of Zoology, University of Toronto, Erindale College, Mississauga, Ontario, Canada.
Exp Cell Res. 1993 Mar;205(1):134-41. doi: 10.1006/excr.1993.1067.
The calcium-dependent regulatory protein calmodulin (CaM) mediates diverse cellular functions via a large number of calmodulin-binding and -dependent proteins (CaMBPs). The use of [35S]calmodulin, labeled during its expression (VU-1-CaM) in Escherichia coli, visualized over 25 CaMBPs in Dictyostelium discoideum. Seven, with M(r)s of 155,000, 91,000, 85,000, 48,000, 46,000, 38,000, and 28,000, were present only during sexual development. In addition, intracellular calmodulin levels were low during gamete formation but rose during cell fusion in response to the presence of extracellular calcium. Thus, calmodulin appears to mediate gamete formation and fusion through two distinct mechanisms: first, via unique developmentally regulated CaMBPs, and, second, via the regulation of intracellular calmodulin levels. The identification of the CaMBP spectrin in sexually developing Dictyostelium cells suggests that this cytoskeleton/plasma membrane, crosslinking protein may function during biomembrane fusion in D. discoideum as it does in other organisms.
钙依赖性调节蛋白钙调蛋白(CaM)通过大量钙调蛋白结合及依赖钙调蛋白的蛋白质(CaMBPs)介导多种细胞功能。利用在大肠杆菌中表达过程中标记的[35S]钙调蛋白(VU-1-CaM),在盘基网柄菌中观察到了超过25种CaMBPs。其中7种蛋白质,分子量分别为155,000、91,000、85,000、48,000、46,000、38,000和28,000,仅在有性发育期间出现。此外,在配子形成过程中细胞内钙调蛋白水平较低,但在细胞融合过程中,由于细胞外钙的存在而升高。因此,钙调蛋白似乎通过两种不同机制介导配子的形成和融合:第一,通过独特的发育调控CaMBPs;第二,通过调节细胞内钙调蛋白水平。在有性发育的盘基网柄菌细胞中鉴定出CaMBP血影蛋白,这表明这种细胞骨架/质膜交联蛋白可能在盘基网柄菌的生物膜融合过程中发挥作用,就像在其他生物体中一样。