MYOSIN-I MOVES ACTIN-FILAMENTS ON A PHOSPHOLIPID SUBSTRATE - IMPLICATIONS FOR MEMBRANE TARGETING

被引:101
作者
ZOT, HG [1 ]
DOBERSTEIN, SK [1 ]
POLLARD, TD [1 ]
机构
[1] JOHNS HOPKINS UNIV, SCH MED, DEPT CELL BIOL & ANAT, BALTIMORE, MD 21205 USA
关键词
D O I
10.1083/jcb.116.2.367
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Acanthamoeba myosin-I bound to substrates of nitrocellulose or planar lipid membranes on glass moved actin filaments at an average velocity of 0.2-mu-m/s. This movement required ATP and phosphorylation of the myosin-I heavy chain. We prepared planar lipid membranes on a glass support by passive fusion of lipid vesicles (Brian, A. A., and H. M. McConnell. 1984. Proc. Natl. Acad. Sci. USA. 81:6159-6163) composed of phosphatidylcholine and containing 0-40% phosphatidylserine. The mass of lipid that bound to the glass was the same for membranes of 2 and 20% phosphatidylserine in phosphatidylcholine and was sufficient to form a single bilayer. Myosin-I moved actin filaments on planar membranes of 5-40% but not 0-2% phosphatidylserine. At the low concentrations of phosphatidylserine, actin filaments tended to detach suggesting that less myosin-I was bound. We used the cooperative activation of Acanthamoeba myosin-I ATPase by low concentrations of actin to assess the association of phospholipids with myosin-I. Under conditions where activity depends on the binding of actin to the tail of myosin-I (Albanesi, J. P., H. Fujisaki, and E. D. Korn. 1985. J. Biol. Chem. 260:11174-11179), phospholipid vesicles with 5-40% phosphatidylserine inhibited ATPase activity. The motility and ATPase results demonstrate a specific interaction of the tail of myosin-I with physiological concentrations of phosphatidylserine. This interaction is sufficient to support motility and may provide a mechanism to target myosin-I to biological membranes.
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页码:367 / 376
页数:10
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