N-terminal acetylation and arginylation of actin determines the architecture and assembly rate of linear and branched actin networks.

ABSTRACT: The great diversity in actin network architectures and dynamics is exploited by cells to drive fundamental biological processes, including cell migration, endocytosis, and cell division. While it is known that this versatility is the result of the many actin-remodeling activities of actin-binding proteins, such as Arp2/3 and cofilin, recent work also implicates posttranslational acetylation or arginylation of the actin N terminus itself as an equally important regulatory mechanism. However, the molecular mechanisms by which acetylation and arginylation alter the properties of actin are not well understood. Here, we directly compare how processing and modification of the N terminus of actin affects its intrinsic polymerization dynamics and its remodeling by actin-binding proteins that are e

SUBMITTER: Chin SM 

PROVIDER: S-EPMC9597890 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature