Optineurin Protein, Human (sf9, His)

Optineurin protein plays a pivotal role in maintaining the Golgi complex, orchestrating membrane trafficking, and regulating exocytosis through its interactions with myosin VI and Rab8. Its linkage of myosin VI to the Golgi complex is integral to Golgi ribbon formation. Furthermore, Optineurin contributes to the activation of the innate immune response during viral infection by recruiting TBK1 to the Golgi apparatus, facilitating its trans-phosphorylation upon stimulation by RLR or TLR3. Activated TBK1, in turn, phosphorylates downstream partner IRF3, leading to the production of IFN-beta/IFNB1. In a neuroprotective role, particularly in the eye and optic nerve, Optineurin regulates membrane trafficking and cellular morphogenesis within a complex involving Rab8 and huntingtin. Additionally, Optineurin serves as an autophagy receptor, interacting with cargo destined for degradation, including ubiquitin-coated bacteria (xenophagy). Notably, it may be targeted by various viruses to inhibit the innate immune response, indicating its multifaceted functions in cellular homeostasis and defense mechanisms.