Structural highlights
FunctionDREB_HUMAN Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.[1] Publication Abstract from PubMedDrebrin modulates F-actin networks and links them to other intracellular components, regulating crucial processes including neuritogenesis, synaptic plasticity, virus internalisation and cancer invasion. Using single-particle cryo-EM we characterise drebrin's interaction with F-actin through two separate conserved actin binding domains (ABD1 and ABD2), revealing structural bases for its F-actin-modulating properties. We describe a multimodal interaction where drebrin's ABD1 can adopt two conformations and a long flexible loop connecting to ABD2 allows the two ABDs to occupy multiple relative positions along F-actin. The flexible loop connecting the two ABDs also confers some propensity to loosely bundle F-actin. Drebrin's ABDs bind across multiple actin protomers and their subdomains and modify the longitudinal inter-protomer interface, explaining its F-actin stabilising properties. Furthermore, we show drebrin's binding site on F-actin is shared with other critical actin-binding and regulatory proteins, explaining their competitive displacement. Structural mechanisms of drebrin-mediated F-actin network modulation.,Zhao W, Chu LY, Abis G, Oozeer F, Mulvaney T, Nagar N, Topf M, Gordon-Weeks PR, Conte MR, Atherton J Nat Commun. 2026 Jun 23;17(1):7894. doi: 10.1038/s41467-026-74543-6. PMID:42337253[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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