» Articles » PMID: 1202021

Organization of an Actin Filament-membrane Complex. Filament Polarity and Membrane Attachment in the Microvilli of Intestinal Epithelial Cells

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1975 Dec 1
PMID 1202021
Citations 220
Authors
Affiliations
Soon will be listed here.
Abstract

The association of actin filaments with membranes is now recognized as an important parameter in the motility of nonmuscle cells. We have investigated the organization of one of the most extensive and highly ordered actin filament-membrane complexes in nature, the brush border of intestinal epithelial cells. Through the analysis of isolated, demembranated brush borders decorated with the myosin subfragment, S1, we have determined that all the microvillar actin filaments have the same polarity. The S1 arrowhead complexes point away from the site of attachment of actin filaments at the apical tip of the microvillar membrane. In addition to the end-on attachment of actin filaments at the tip of the microvillus, these filaments are also connected to the plasma membrane all along their lengths by periodic (33 nm) cross bridges. These bridges were best observed in isolated brush borders incubated in high concentrations of Mg++. Their visibility is attributed to the induction of actin paracrystals in the filament bundles of the microvilli. Finally, we present evidence for the presence of myosinlike filaments in the terminal web region of the brush border. A model for the functional organization of actin and myosin in the brush border is presented.

Citing Articles

Prominosomes - a particular class of extracellular vesicles containing prominin-1/CD133?.

Karbanova J, Thamm K, Fargeas C, Deniz I, Lorico A, Corbeil D J Nanobiotechnology. 2025; 23(1):61.

PMID: 39881297 PMC: 11776279. DOI: 10.1186/s12951-025-03102-w.


Organization of a cytoskeletal superstructure in the apical domain of intestinal tuft cells.

Silverman J, Krystofiak E, Caplan L, Lau K, Tyska M J Cell Biol. 2024; 223(12).

PMID: 39352498 PMC: 11457492. DOI: 10.1083/jcb.202404070.


Actin cytoskeleton and associated myosin motors within the renal epithelium.

Busselman B, Ratnayake I, Terasaki M, Thakkar V, Ilyas A, Otterpohl K Am J Physiol Renal Physiol. 2024; 327(4):F553-F565.

PMID: 39052845 PMC: 11483076. DOI: 10.1152/ajprenal.00078.2024.


Modeling the cell biology of monogenetic intestinal epithelial disorders.

Kaji I, Thiagarajah J, Goldenring J J Cell Biol. 2024; 223(7).

PMID: 38683247 PMC: 11058565. DOI: 10.1083/jcb.202310118.


Discovery of the first unconventional myosin: myosin-I.

Pollard T, Korn E Front Physiol. 2023; 14:1324623.

PMID: 38046947 PMC: 10693453. DOI: 10.3389/fphys.2023.1324623.


References
1.
Gruenstein E, Rich A, Weihing R . Actin associated with membranes from 3T3 mouse fibroblast and HeLa cells. J Cell Biol. 1975; 64(1):223-34. PMC: 2109470. DOI: 10.1083/jcb.64.1.223. View

2.
Tilney L . Actin filaments in the acrosomal reaction of Limulus sperm. Motion generated by alterations in the packing of the filaments. J Cell Biol. 1975; 64(2):289-310. PMC: 2109505. DOI: 10.1083/jcb.64.2.289. View

3.
Palevitz B, Hepler P . Identification of actin in situ at the ectoplasm-endoplasm interface of Nitella. Microfilament-chloroplast association. J Cell Biol. 1975; 65(1):29-38. PMC: 2111164. DOI: 10.1083/jcb.65.1.29. View

4.
Podlubnaya Z, Tskhovrebova L, Zaalishtsbvili M, Stefanenko G . Electron microscopic study of alpha-actinin. J Mol Biol. 1975; 92(2):357-9. DOI: 10.1016/0022-2836(75)90234-x. View

5.
Perry M, John H, Thomas N . Actin-like filaments in the cleavage furrow of newt egg. Exp Cell Res. 1971; 65(1):249-53. DOI: 10.1016/s0014-4827(71)80075-7. View