8COG
Human arginylated beta-actin
Summary for 8COG
| Entry DOI | 10.2210/pdb8cog/pdb |
| EMDB information | 16776 |
| Descriptor | Actin, cytoplasmic 1, N-terminally processed, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | actin, methylated, filament, contractile protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 42158.10 |
| Authors | Pinto, C.S.,Bakker, S.E.,Suchenko, A.,Hussain, H.,Hatano, T.,Sampath, K.,Chinthalapudi, K.,Mishima, M.,Balasubramanian, M. (deposition date: 2023-02-28, release date: 2024-03-06, Last modification date: 2025-12-17) |
| Primary citation | Pinto, C.S.,Bakker, S.E.,Suchenko, A.,Kolodny, I.M.,Hussain, H.,Hatano, T.,Sampath, K.,Chinthalapudi, K.,Heissler, S.M.,Mishima, M.,Balasubramanian, M. Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation. J.Cell Biol., 225:-, 2026 Cited by PubMed Abstract: 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. PubMed: 41236477DOI: 10.1083/jcb.202409067 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.499 Å) |
Structure validation
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