Structural highlights
Function
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [CAP1_MOUSE] Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity.
Publication Abstract from PubMed
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.
Structural basis of actin monomer re-charging by cyclase-associated protein.,Kotila T, Kogan K, Enkavi G, Guo S, Vattulainen I, Goode BL, Lappalainen P Nat Commun. 2018 May 14;9(1):1892. doi: 10.1038/s41467-018-04231-7. PMID:29760438[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kotila T, Kogan K, Enkavi G, Guo S, Vattulainen I, Goode BL, Lappalainen P. Structural basis of actin monomer re-charging by cyclase-associated protein. Nat Commun. 2018 May 14;9(1):1892. doi: 10.1038/s41467-018-04231-7. PMID:29760438 doi:http://dx.doi.org/10.1038/s41467-018-04231-7
