The success of cell division to equally segregate genetic materials into two daughter cells depends on the constriction of actomyosin-based contractile ring. The spatial and temporal regulation of contractile ring at the division plane primarily depends on two parallel intracellular signals, centralspindlin-dependent and astral relaxation pathways, in which both of them are studied extensively. However, the extracellular signal that regulates cytokinetic processes is poorly investigated. Up to now, only hemicentin (HIM-4), an extracellular matrix protein, has been showed may regulate cytokinesis in mouse embryos and C. elegans germline. Depletion of HIM-4 in both model organisms leads to multinucleated cells. However, the molecular mechanism of HIM-4 in cytokinesis regulation is still not clear. In this study, we demonstrate that HIM-4 is recruited to the site of cleavage furrow and promotes proper cytokinesis in C. elegans germ cell. The timing of contractile ring formation and cleavage furrow closure is greatly delayed in HIM-4-depleted germ cells. In addition, the recruitment and dynamic of ANI-1 is reduced in HIM-4-depleted gonad, while non-muscle myosin (NMY-2) and ANI-2 remain unchanged. Collectively, our data suggest that HIM-4 may regulate cytokinesis by promoting and stabilizing ANI-1 to the site of division in C. elegans germ cells.