Posas F, Takekawa M, Saito H
Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street,Boston, MA 02115, USA.
Curr Opin Microbiol. 1998 Apr;1(2):175-82. doi: 10.1016/s1369-5274(98)80008-8.
Budding yeast contain at least four distinct MAPK (mitogen activated protein kinase) cascades that transduce a variety of intracellular signals: mating-pheromone response, pseudohyphal/invasive growth, cell wall integrity, and high osmolarity adaptation. Although each MAPK cascade contains a conserved set of three protein kinases, the upstream activation mechanisms for these cascades are diverse, including a trimeric G protein, monomeric small G proteins, and a prokaryotic-like two-component system. Recently, it became apparent that there is extensive sharing of signaling elements among the MAPK pathways; however, little undesirable cross-talk occurs between various cascades. The formation of multi-protein signaling complexes is probably centrally important for this insulation of individual MAPK cascades.
芽殖酵母至少含有四种不同的丝裂原活化蛋白激酶（MAPK）级联反应，它们可转导多种细胞内信号：交配信息素反应、假菌丝/侵袭性生长、细胞壁完整性和高渗透压适应性。尽管每个MAPK级联反应都包含一组保守的三种蛋白激酶，但这些级联反应的上游激活机制多种多样，包括三聚体G蛋白、单体小G蛋白和原核生物样双组分系统。最近，很明显MAPK途径之间存在广泛的信号元件共享；然而，不同级联反应之间几乎没有不良的串扰。多蛋白信号复合物的形成可能对单个MAPK级联反应的这种隔离至关重要。
