Unknown

Dataset Information

0

Actin filaments partition primary cilia membranes into distinct fluid corrals.


ABSTRACT: Physical properties of primary cilia membranes in living cells were examined using two independent, high-spatiotemporal-resolution approaches: fast tracking of single quantum dot-labeled G protein-coupled receptors and a novel two-photon super-resolution fluorescence recovery after photobleaching of protein ensemble. Both approaches demonstrated the cilium membrane to be partitioned into corralled domains spanning 274 ± 20 nm, within which the receptors are transiently confined for 0.71 ± 0.09 s. The mean membrane diffusion coefficient within the corrals, Dm1 = 2.9 ± 0.41 µm2/s, showed that the ciliary membranes were among the most fluid encountered. At longer times, the apparent membrane diffusion coefficient, Dm2 = 0.23 ± 0.05 µm2/s, showed that corral boundaries impeded receptor diffusion 13-fold. Mathematical simulations predict the probability of G protein-coupled receptors crossing corral boundaries to be 1 in 472. Remarkably, latrunculin A, cytochalasin D, and jasplakinolide treatments altered the corral permeability. Ciliary membranes are thus partitioned into highly fluid membrane nanodomains that are delimited by filamentous actin.

SUBMITTER: Lee S 

PROVIDER: S-EPMC6080922 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC8017684 | biostudies-literature
| S-EPMC7725934 | biostudies-literature
| S-EPMC10824913 | biostudies-literature
| S-EPMC4133290 | biostudies-literature
| S-EPMC9689266 | biostudies-literature
| S-EPMC3226981 | biostudies-literature
| S-EPMC10916631 | biostudies-literature
| S-EPMC5530675 | biostudies-literature
| S-EPMC3277726 | biostudies-literature
| S-EPMC2575454 | biostudies-literature