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TitleActin arginylation alters myosin engagement and F-actin patterning despite structural conservation.
Journal, issue, pagesJ Cell Biol, Vol. 225, Issue 1, Year 2026
Publish dateJan 5, 2026
AuthorsClyde Savio Pinto / Saskia E Bakker / Andrejus Suchenko / Isabella M Kolodny / Hamdi Hussain / Tomoyuki Hatano / Karuna Sampath / Krishna Chinthalapudi / Sarah M Heissler / Masanori Mishima / Mohan Balasubramanian /
PubMed AbstractActin is a conserved protein with crucial roles in cell polarity, division, and muscle contraction. Its function is regulated in part by posttranslational modifications, one of which is N-terminal ...Actin is a conserved protein with crucial roles in cell polarity, division, and muscle contraction. Its function is regulated in part by posttranslational modifications, one of which is N-terminal arginylation. What is the structure of arginylated-β-actin (R-β-actin), and how does it regulate F-actin function? Here we report the 3.6 Å structures of ADP-R-β-actin filaments, which are nearly identical to that of non-arginylated F-actin. In vitro assays reveal that the interaction between myosin-II and actin is altered upon actin arginylation, characterized by frequent detachment of R-actin filaments from myosin-II. In vivo, replacement of the only actin gene in Schizosaccharomyces pombe with a synthetic gene encoding R-Sp-actin reduces Arp2/3-based actin patches while thickening formin-induced actin cables. Consistent with defective interactions between myosin-II and R-actin filaments, assembly and constriction of the cytokinetic actomyosin ring are perturbed in R-Sp-actin cells. Thus, despite structural similarity of arginylated and non-arginylated actin filaments, actin arginylation affects F-actin assortment into distinct subcellular structures and its interaction with myosin-II.
External linksJ Cell Biol / PubMed:41236477 / PubMed Central
MethodsEM (single particle)
Resolution3.499 Å
Structure data

16776

8cog

EMDB-16776, PDB-8cog:
Human arginylated beta-actin
Method: EM (single particle) / Resolution: 3.499 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCONTRACTILE PROTEIN / actin / methylated / filament

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