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ATPase activity of the microvillar 110 kDa polypeptide-calmodulin complex is activated in Mg2+ and inhibited in K+-EDTA by F-actin.

作者信息

Krizek J, Coluccio L M, Bretscher A

机构信息

Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.

出版信息

FEBS Lett. 1987 Dec 10;225(1-2):269-72. doi: 10.1016/0014-5793(87)81172-9.

DOI:10.1016/0014-5793(87)81172-9
PMID:2961614
Abstract

Highly purified microvillar 110 kDa polypeptide-calmodulin (110K-cam) complex was confirmed to have ATPase activities characteristic of a myosin. The effect of F-actin on these activities was investigated. The Mg2+-ATPase is activated about 2-fold by F-actin in a dose-dependent fashion, whereas the K+-EDTA-ATPase is inhibited by greater than 90% by F-actin. These data provide evidence for a functional relationship between the ATPase activity of 110K-cam and its interaction with F-actin. They also extend the similarities between 110K-cam and myosin. The results suggest that higher cells contain in addition to myosin a second class of myosin-like molecules represented by 110K-cam.

摘要

相似文献

1
ATPase activity of the microvillar 110 kDa polypeptide-calmodulin complex is activated in Mg2+ and inhibited in K+-EDTA by F-actin.
FEBS Lett. 1987 Dec 10;225(1-2):269-72. doi: 10.1016/0014-5793(87)81172-9.
2
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6
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10
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引用本文的文献

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J Bacteriol. 1993 Apr;175(8):2189-96. doi: 10.1128/jb.175.8.2189-2196.1993.
2
Reassociation of microvillar core proteins: making a microvillar core in vitro.微绒毛核心蛋白的重新缔合：体外构建微绒毛核心
J Cell Biol. 1989 Feb;108(2):495-502. doi: 10.1083/jcb.108.2.495.
3
Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.
禽类肠道微绒毛110-kD钙调蛋白复合体的部分推导序列表明，这种机械酶是肌球蛋白I家族的成员。
J Cell Biol. 1989 Dec;109(6 Pt 1):2895-903. doi: 10.1083/jcb.109.6.2895.
4
Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor.埃兹蛋白和血影蛋白的快速磷酸化及重排伴随着表皮生长因子诱导A-431细胞发生的形态变化。
J Cell Biol. 1989 Mar;108(3):921-30. doi: 10.1083/jcb.108.3.921.
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Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).肠微绒毛膜盘的特性：富含相关刷状缘肌球蛋白I（110K-钙调蛋白）的抗去污剂膜片。
J Cell Biol. 1989 Sep;109(3):1153-61. doi: 10.1083/jcb.109.3.1153.
6
The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.肠道微绒毛（刷状缘肌球蛋白I）的110-kD蛋白质-钙调蛋白复合物是一种机械酶。
J Cell Biol. 1989 Jun;108(6):2395-400. doi: 10.1083/jcb.108.6.2395.
7
Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains.肠道微绒毛110K-钙调蛋白复合物中110-kD肌球蛋白样亚基的结构与免疫学特性：离散肌球蛋白头部和钙调蛋白结合结构域的证据
J Cell Biol. 1988 Nov;107(5):1749-57. doi: 10.1083/jcb.107.5.1749.
8
Binding of brush border myosin I to phospholipid vesicles.刷状缘肌球蛋白I与磷脂囊泡的结合。
J Cell Biol. 1990 Aug;111(2):443-51. doi: 10.1083/jcb.111.2.443.
9
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