Unknown

Dataset Information

0

Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement.


ABSTRACT: Ankyrin-repeat domains (ARDs) are conserved in large numbers of proteins. ARDs are composed of various numbers of ankyrin repeats (ANKs). ARDs often adopt curved structures reminiscent of the Bin-Amphiphysin-Rvs (BAR) domain, which is the dimeric scaffold for membrane tubulation. BAR domains sometimes have amphipathic helices for membrane tubulation and vesiculation. However, it is unclear whether ARD-containing proteins exhibit similar membrane deformation properties. We found that the ARD of ANK and KH domain-containing protein 1 (ANKHD1) dimerize and deform membranes into tubules and vesicles. Among 25 ANKs of ANKHD1, the first 15 ANKs can form a dimer and the latter 10 ANKs enable membrane tubulation and vesiculation through an adjacent amphipathic helix and a predicted curved structure with a positively charged surface, analogous to BAR domains. Knockdown and localization of ANKHD1 suggested its involvement in the negative regulation of early endosome enlargement owing to its membrane vesiculation.

SUBMITTER: Kitamata M 

PROVIDER: S-EPMC6606961 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC2592678 | biostudies-literature
| S-EPMC2175155 | biostudies-literature
| S-EPMC3376135 | biostudies-literature
| S-EPMC8624802 | biostudies-literature
2020-09-25 | GSE157349 | GEO
| S-SCDT-10_15252-EMBR_202256538 | biostudies-other
| S-EPMC3820240 | biostudies-literature
| S-EPMC3912533 | biostudies-literature
| S-EPMC6453936 | biostudies-literature
| S-EPMC3517540 | biostudies-literature