King Stephen M
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305, USA.
Sci Signal. 2008 Nov 25;1(47):pe51. doi: 10.1126/scisignal.147pe51.
The highly conserved DYNLL/LC8 proteins promote dimerization of a broad range of targets and are essential for the integrity, activity, or both, of many subcellular systems, such as dyneins, myosin V, and apoptotic factors. Defects in DYNLL/LC8 function lead to severe cellular and developmental phenotypes in multicellular organisms, whereas loss-of-function alleles are lethal. DYNLL/LC8 dimer formation may be controlled by various signaling inputs (including pH changes and phosphorylation), and dimerization has been linked to alterations in the enzymatic activity of neuronal nitric oxide synthase and apoptotic control. A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-kappaB.
高度保守的DYNLL/LC8蛋白可促进多种靶标的二聚化，并且对于许多亚细胞系统（如动力蛋白、肌球蛋白V和凋亡因子）的完整性、活性或两者兼具而言至关重要。DYNLL/LC8功能缺陷会导致多细胞生物体出现严重的细胞和发育表型，而功能丧失等位基因是致死性的。DYNLL/LC8二聚体的形成可能受多种信号输入（包括pH变化和磷酸化）的控制，并且二聚化与神经元型一氧化氮合酶的酶活性改变和凋亡调控有关。最近的一份报告提出，DYNLL/LC8驱动的相互作用也受细胞氧化还原状态变化的调节，这种变化会导致单体间二硫键形成，并最终激活转录因子NF-κB。
