Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260-1300, USA.
Curr Biol. 2010 Aug 10;20(15):1389-95. doi: 10.1016/j.cub.2010.06.033. Epub 2010 Jul 8.
Cell adhesion is a key feature in the regulation of many biological processes. In the budding yeast Saccharomyces cerevisiae, Flo11p is the major adhesion molecule that controls filamentous growth [1-3] and the expansion of interconnected cells in mats or biofilms [4]. We show here that Flo11p is shed from cells. Flo11p shedding attenuated adherence and contributed to the overall balance in adherence properties that was optimal for filamentous growth and mat formation. Shed Flo11p comprised an essential component of a fluid layer surrounding yeast mats that may be functionally analogous to the mucus secretions of higher eukaryotes. Genome-wide secretion profiling of Flo11p identified new regulatory proteins, including the furin protease Kex2p, which was required for cleavage and maturation of the Flo11p protein. Secreted mucin-like proteins may play unexpected roles in the adherence properties and virulence of microbial pathogens.
细胞黏附是调控许多生物学过程的关键特征。在出芽酵母酿酒酵母中，Flo11p 是主要的黏附分子，它控制丝状生长[1-3]和细胞在垫或生物膜中的相互连接的扩展[4]。我们在这里显示 Flo11p 从细胞中脱落。Flo11p 的脱落减弱了黏附性，并有助于整体平衡黏附特性，这对于丝状生长和垫形成是最佳的。脱落的 Flo11p 构成了围绕酵母垫的流体层的一个必需组成部分，该层可能在功能上类似于高等真核生物的粘液分泌物。Flo11p 的全基因组分泌谱分析鉴定了新的调节蛋白，包括参与 Flo11p 蛋白切割和成熟的弗林蛋白酶 Kex2p。分泌的粘蛋白样蛋白可能在微生物病原体的黏附特性和毒力中发挥意想不到的作用。
