Search Within
hpa027398
Keyword:'hpa027398'
Showing 1-6 of 6 results for "hpa027398" within Papers
The Journal of biological chemistry, 295(48), 16191-16206 (2020-10-15)
Solute transporting epithelial cells build arrays of microvilli on their apical surface to increase membrane scaffolding capacity and enhance function potential. In epithelial tissues such as the kidney and gut, microvilli are length-matched and assembled into tightly packed "brush borders,"
Developmental cell, 36(2), 190-200 (2016-01-27)
Transporting and sensory epithelial cells shape apical specializations using protocadherin-based adhesion. In the enterocyte brush border, protocadherin function requires a complex of cytoplasmic binding partners, although the composition of this complex and logic governing its assembly remain poorly understood. We
Molecular biology of the cell, 30(1), 108-118 (2018-11-08)
Transporting epithelial cells optimize their morphology for solute uptake by building an apical specialization: a dense array of microvilli that serves to increase membrane surface area. In the intestinal tract, individual cells build thousands of microvilli, which pack tightly to
The Journal of biological chemistry, 295(28), 9281-9296 (2020-03-27)
Specialized transporting and sensory epithelial cells employ homologous protocadherin-based adhesion complexes to remodel their apical membrane protrusions into organized functional arrays. Within the intestine, the nutrient-transporting enterocytes utilize the intermicrovillar adhesion complex (IMAC) to assemble their apical microvilli into an
The Journal of biological chemistry, 295(36), 12588-12604 (2020-07-09)
Nutrient-transporting enterocytes interact with their luminal environment using a densely packed collection of apical microvilli known as the brush border. Assembly of the brush border is controlled by the intermicrovillar adhesion complex (IMAC), a protocadherin-based complex found at the tips
Proceedings of the National Academy of Sciences of the United States of America, 114(19), E3776-E3785 (2017-04-26)
Unconventional myosin 7a (Myo7a), myosin 7b (Myo7b), and myosin 15a (Myo15a) all contain MyTH4-FERM domains (myosin tail homology 4-band 4.1, ezrin, radixin, moesin; MF) in their cargo binding tails and are essential for the growth and function of microvilli and
Page 1 of 1