An extracellular matrix protein promotes anillin-dependent processes in the Caenorhabditis elegans germline

An extracellular matrix protein promotes anillin-dependent processes in the Caenorhabditis elegans germline
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细胞外基质蛋白促进秀丽隐杆线虫种系中的苯胺依赖性过程

DOI:
10.26508/lsa.201800152
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发表时间:
2019-04
影响因子:
4.4
通讯作者:
Tse Yu Chung
Tse Yu Chung
中科院分区:
生物学2区
文献类型:
--
作者:
Lan Hongxia;Wang Xinyan;Jiang Ling;Wu Jianjian;Wan Xuan;Zeng Lidan;Zhang D;an;Lin Yiyan;Hou Chunhui;Wu Shian;Tse Yu Chung

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The extracellular matrix protein Hemicentin (HIM-4) is an extracellular factor that regulates anillin (ANI-1) for germ cell membrane stabilization and contractile ring formation in C. elegans germline cells. Cell division requires constriction of an actomyosin ring to segregate the genetic material equally into two daughter cells. The spatial and temporal regulation of the contractile ring at the division plane primarily depends on intracellular signals mediated by the centralspindlin complex and astral microtubules. Although much investigative work has elucidated intracellular factors and mechanisms controlling this process, the extracellular regulation of cytokinesis remains unclear. Thus far, the extracellular matrix protein Hemicentin (HIM-4) has been proposed to be required for cleavage furrow stabilization. The underlying molecular mechanism, however, has remained largely unknown. Here, we show that HIM-4 and anillin (ANI-1) genetically act in the same pathway to maintain the rachis bridge stability in the germline. Our FRAP experiments further reveal that HIM-4 restricts the motility of ANI-1. In addition, we demonstrate that HIM-4 is recruited to the cleavage site in dividing germ cells and promotes the proper ingression of the cleavage membrane. Collectively, we propose that HIM-4 is an extracellular factor that regulates ANI-1 for germ cell membrane stabilization and contractile ring formation in Caenorhabditis elegans germline cells.
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影响因子: 3.5
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