Unknown

Dataset Information

0

Micrographs that led to the structure of Dia1 on F-actin


ABSTRACT:

SUBMITTER: Roberto Dominguez 

PROVIDER: EMPIAR-12455 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

Mechanisms of actin filament severing and elongation by formins.

Palmer Nicholas J NJ   Barrie Kyle R KR   Dominguez Roberto R  

Nature 20240606 8024


Humans express 15 formins that play crucial roles in actin-based processes, including cytokinesis, cell motility and mechanotransduction<sup>1,2</sup>. However, the lack of structures bound to the actin filament (F-actin) has been a major impediment to understanding formin function. Whereas formins are known for their ability to nucleate and elongate F-actin<sup>3-7</sup>, some formins can additionally depolymerize, sever or bundle F-actin. Two mammalian formins, inverted formin 2 (INF2) and dia  ...[more]

Similar Datasets

| EMPIAR-13421 | biostudies-other
| EMPIAR-13294 | biostudies-other
| EMPIAR-12243 | biostudies-other
2024-04-12 | GSE242945 | GEO
2024-04-12 | GSE242944 | GEO
2024-04-12 | GSE242943 | GEO
| PRJNA1015586 | ENA
| S-EPMC3130349 | biostudies-literature
| S-EPMC2781601 | biostudies-literature