Structural basis of actin monomer re-charging by cyclase-associated protein View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Tommi Kotila, Konstantin Kogan, Giray Enkavi, Siyang Guo, Ilpo Vattulainen, Bruce L. Goode, Pekka Lappalainen

ABSTRACT

Actin polymerization powers key cellular processes, including motility, morphogenesis, and endocytosis. The actin turnover cycle depends critically on "re-charging" of ADP-actin monomers with ATP, but whether this reaction requires dedicated proteins in cells, and the underlying mechanism, have remained elusive. Here we report that nucleotide exchange catalyzed by the ubiquitous cytoskeletal regulator cyclase-associated protein (CAP) is critical for actin-based processes in vivo. We determine the structure of the CAP-actin complex, which reveals that nucleotide exchange occurs in a compact, sandwich-like complex formed between the dimeric actin-binding domain of CAP and two ADP-actin monomers. In the crystal structure, the C-terminal tail of CAP associates with the nucleotide-sensing region of actin, and this interaction is required for rapid re-charging of actin by both yeast and mammalian CAPs. These data uncover the conserved structural basis and biological role of protein-catalyzed re-charging of actin monomers. More... »

PAGES

1892

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-018-04231-7

DOI

http://dx.doi.org/10.1038/s41467-018-04231-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1103889239

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29760438


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