RGD Reference Report - A role for myosin-1A in the localization of a brush border disaccharidase. - Rat Genome Database
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A role for myosin-1A in the localization of a brush border disaccharidase.

Authors: Tyska, MJ  Mooseker, MS 
Citation: Tyska MJ and Mooseker MS, J Cell Biol. 2004 May 10;165(3):395-405.
RGD ID: 1581729
Pubmed: (View Article at PubMed) PMID:15138292
DOI: Full-text: DOI:10.1083/jcb.200310031

To gain insight regarding myosin-1A (M1A) function, we expressed a dominant negative fragment of this motor in the intestinal epithelial cell line, CACO-2BBE. 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-2BBE cells and rat microvilli (MV) all indicate that M1A and SI reside on the same population of low density (approximately 1.12 g/ml) membranes. Chemical cross-linking of detergent-resistant membranes from rat MV 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.


Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Myo1a  (myosin IA)
Si  (sucrase-isomaltase)

Additional Information