Turnover of the actomyosin complex in zebrafish embryos directs geometric remodelling and the recruitment of lipid droplets.
Lipid droplets (LDs), reservoirs of cholesterols and fats, are organelles that hydrolyse lipids in the cell. In zebrafish embryos, the actomyosin complex and filamentous microtubules control the periodic regulation of the LD geometry. Contrary to the existing hypothesis that LD transport involves the kinesin-microtubule system, we find that their recruitment to the blastodisc depends on the actomyosin turnover and is independent of the microtubules. For the first time we report the existence of two distinct states of LDs, an inactive and an active state, that occur periodically, coupled weakly to the cleavage cycles. LDs are bigger, more circular and more stable in the inactive state in which the geometry of the LDs is maintained by actomyosin as well as microtubules. The active state has smaller and irregularly shaped LDs that show shape fluctuations that are linked to actin depolymerization. Because most functions of LDs employ surface interactions, our findings on the LD geometry and its regulation bring new insights to the mechanisms associated with specific functions of LDs, such as their storage capacity for fats or proteins, lipolysis etc.
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata; 700032, India.
Asmita
A
Dutta
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata; 700032, India.
Deepak
D
Kumar Sinha
D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004625:Embryo, Nonmammalian; D047108:Embryonic Development; D066292:Lipid Droplets / Q000378:metabolism*; D050356:Lipid Metabolism; D008870:Microtubules / Q000378:metabolism; D024462:Myosin Type II / Q000378:metabolism; D055550:Protein Stability; D015027:Zebrafish / Q000196:embryology / Q000378:metabolism*
D000199:Actins; D000205:Actomyosin; D024462:Myosin Type II