期刊
JOURNAL OF CELL BIOLOGY
卷 177, 期 4, 页码 671-681出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200701144
关键词
-
类别
资金
- NICHD NIH HHS [T32 HD007502, HD07502] Funding Source: Medline
- NIDDK NIH HHS [R01 DK075555, DK075555] Funding Source: Medline
Microvilli are actin-rich membrane protrusions common to a variety of epithelial cell types. Within microvilli of the enterocyte brush border (BB), myosin-1a (Myo1a) forms an ordered ensemble of bridges that link the plasma membrane to the underlying polarized actin bundle. Despite decades of investigation, the function of this unique actomyosin array has remained unclear. Here, we show that addition of ATP to isolated BBs induces a plus end-directed translation of apical membrane along microvillar actin bundles. Upon reaching microvillar tips, membrane is shed into solution in the form of small vesicles. Because this movement demonstrates the polarity, velocity, and nucleotide dependence expected for a Myo1a- driven process, and BBs lacking Myo1a fail to undergo membrane translation, we conclude that Myo1a powers this novel form of motility. Thus, in addition to providing a means for amplifying apical surface area, we propose that microvilli function as actomyosin contractile arrays that power the release of BB membrane vesicles into the intestinal lumen.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据