Abstract
AbstractIntracellular membrane tubules play a crucial role in diverse cellular processes, and their regulation is facilitated by Bin-Amphiphysin-Rvs (BAR) domain-containing proteins. This study investigates the roles of dICA69N-BARand dCIP4F-BARin vivo, focusing on their impact onin vivotubule organization. Through cell culture and immunofluorescence staining, we observed co-localization of endogenous dICA69 with dCIP4-induced membrane tubules, indicating their potential recruitment for tubule formation and maintenance. Additionally, dCIP4-positive tubules exhibit enrichment of actin regulatory proteins such as Wasp, SCAR, Arp2, Arp3, and Syndapin. Overexpressing dICA69N-BARin S2R+ cells reveals distinct punctate patterns in the perinuclear region. An earlier study indicated that F-BAR proteins spontaneously segregate from the N-BAR domain-containing proteins during membrane tubule formation. In contrast, our observation supports a model in which different BAR-domain family members can associate with the same tubule and cooperate to fine-tune the tubule width. Moreover, our analysis highlights how dCIP4F-BARfacilitates the redistribution of dICA69N-BARpunctae, leading to altered patterns within the cells. These cooperative activities of dICA69N-BARand dCIP4F-BARare vital for the precise organization of intracellular tubules. Understanding the underlying mechanisms governing this cooperation provides valuable insights into cellular dynamics and the organization of membrane tubules. The implications extend to various physiological and pathological conditions related to intracellular membrane dynamics.
Publisher
Cold Spring Harbor Laboratory
Cited by
2 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献