预约演示

更新于：2025-05-07

ANLN

更新于：2025-05-07

基本信息

别名

ANILLIN、anillin actin binding protein、ANLN

+ [2]

简介

Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636).

关联

项与 ANLN 相关的药物

CN116875598

专利挖掘

靶点

ANLN

作用机制-

在研机构

暨南大学

原研机构

暨南大学

在研适应症

肿瘤 [+1]

非在研适应症-

最高研发阶段药物发现

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 ANLN 相关的临床结果

登录后查看更多信息

100 项与 ANLN 相关的转化医学

登录后查看更多信息

0 项与 ANLN 相关的专利（医药）

登录后查看更多信息

595

项与 ANLN 相关的文献（医药）

2025-06-02·Journal of Cell Biology

Anillin mediates unilateral furrowing during cytokinesis by limiting RhoA binding to its effectors

Article

作者: Zanin, Esther ; Lebedev, Mikhail ; Bellessem, Jennifer ; Chan, Fung-Yi ; Mikeladze-Dvali, Tamara ; Rackles, Elisabeth ; Xavier Carvalho, Ana

During unilateral furrow ingression, one side of the cytokinetic ring (leading edge) ingresses before the opposite side (lagging edge). Anillin mediates unilateral furrowing during cytokinesis in the one-cell C. elegans zygote by limiting myosin II accumulation in the ring. Here, we address the role of anillin in this process and show that anillin inhibits not only the accumulation of myosin II but also of other RhoA effectors by binding and blocking the RhoA effector site. The interaction between the anillin’s RhoA-binding domain (RBD) and active RhoA is enhanced by the disordered linker region and differentially regulated at the leading and lagging edge, which together results in asymmetric RhoA signaling and accumulation of myosin II. In summary, we discover a RhoA GEF- and GAP-independent mechanism, where RhoA activity is limited by anillin binding to the RhoA effector site. Spatial fine-tuning of anillin’s inhibitory role on RhoA signaling enables unilateral furrow ingression and contributes to animal development.

2025-06-01·Biofilm

Sucrose reduces biofilm formation by Klebsiella pneumoniae through the PTS components ScrA and Crr

Article

作者: Chen, Yih-Yuan ; Tseng, Shih-Wen ; Chien, Chih-Ching ; Horng, Yu-Tze ; Chen, Hsueh-Wen ; Soo, Po-Chi ; Dewi Panjaitan, Novaria Sari ; Yang, Hung-Chi

The presence of sucrose at concentrations of 0.5-5% can either increase bacterial biofilms (Streptococcus mutans and Escherichia coli) or have no significant effect on biofilms (Pseudomonas aeruginosa and Staphylococcus aureus). However, our study revealed that 1 % sucrose reduced the biofilm formation by Klebsiella pneumoniae STU1. To explore the role of the phosphoenolpyruvate-dependent-carbohydrate: phosphotransferase system (PTS) in regulating this process, the scrA gene, which encodes the sucrose-specific EIIBC of the PTS, was deleted in K. pneumoniae to create a scrA mutant (ΔscrA). Thereafter, we observed that the biofilm formation and type 3 fimbriae production were not affected by sucrose in the ΔscrA while sucrose reduced these processes in the wild type. Furthermore, we discovered that Crr, the glucose-specific EIIA of PTS, was the primary but not the sole EIIA of ScrA in K. pneumoniae by sucrose fermentation test. In addition, deficiency of Crr reduced the biofilm formation in K. pneumoniae. Our proposed model suggests that, through the action of Crr in the absence of sucrose, the transcription of the mrk operon, which produces type 3 fimbriae, was increased, thereby influencing biofilm formation by K. pneumoniae and bacterial number in the gut of nematode. This observation differs from the regulation of polysaccharide and biofilm by sucrose in other bacteria. Our findings extend the understanding of the effects of sucrose on biofilm formation.

2025-04-01·Cytoskeleton

Septin complexes: Ahead of the curve

Review

作者: Nakamura, Mitsutoshi ; Parkhurst, Susan M.

AbstractIndividual cells have robust repair systems to survive cell cortex damage caused by mechanical and chemical stresses, allowing them to maintain the integrity of tissues and organs. The contraction of an actomyosin ring at the wound edge is a major mechanism for physically closing the cell wound. In contrast to polymerization and bundling of actin filaments, little is known about how linear actin filaments are bent to be integrated into the actin ring structure encircling the wound edge. We recently found that the five Drosophila Septins function simultaneously in the regulation of actomyosin ring assembly, contraction, and disassembly during cell wound repair. These Septins form two distinct complexes—Sep1‐Sep2‐Pnut and Sep4‐Sep5‐Pnut—composed of different subunits from the same groups. Strikingly, these two distinct Septin complexes have different degrees of F‐actin bending activities that are consistent with their spatial recruitment: different degrees of curved actin filaments are required for the robust formation of different regions of the actomyosin ring. In addition, we found that the two Septin complexes are regulated by different molecular pathways as a loss of Anillin only affects Sep1‐Sep2‐Pnut complex recruitment. These findings open new directions for how individual Septin subunits form complexes and function differentially in cellular and developmental processes.

分析

对领域进行一次全面的分析。

或

查看完整样例数据

Eureka LS:

全新生物医药AI Agent 覆盖科研全链路，让突破性发现快人一步

立即开始免费试用!

智慧芽新药情报库是智慧芽专为生命科学人士构建的基于AI的创新药情报平台，助您全方位提升您的研发与决策效率。

立即开始数据试用!

智慧芽新药库数据也通过智慧芽数据服务平台，以API或者数据包形式对外开放，助您更加充分利用智慧芽新药情报信息。