期刊
JOURNAL OF CELL BIOLOGY
卷 165, 期 3, 页码 395-405出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200310031
关键词
actin; membrane; lipid raft; microvillus; epithelium
类别
资金
- NIDDK NIH HHS [DK-10113, DK-55389, DK-25387, P01 DK055389, R37 DK025387, R56 DK025387, F32 DK010113, R01 DK025387] Funding Source: Medline
To gain insight regarding myosin-1A (MIA) function, we expressed a dominant negative fragment of this motor in the intestinal epithelial cell line, CACO-2(BBE). Sucrase isomaltase (SI), a transmembrane disaccharidase found in microvillar lipid rafts, was missing from the brush border (BB) in cells expressing this fragment. Density gradient centrifugation, affinity purification, and immunopurification of detergent-resistant membranes isolated from CACO-2(BBE) cells and rat microvilli (MV) all indicate that M1A and SI reside on the same population of low density (similar to1.12 g/ml) membranes. Chemical cross-linking of detergent-resistant membranes from rat MY indicates that SI and M1A may interact in a lipid raft complex. The functional significance of such a complex is highlighted by expression of the cytoplasmic domain of SI, which results in lower levels of M1A and a loss of SI from the BB. Together, these studies are the first to assign a specific role to M1A and suggest that this motor is involved in the retention of SI within the BB.
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