Nature Structural &amp; Molecular Biology

dlvr.itMolecular control of bacterial immunityNature Structural & Molecular Biology, Published online: 21 October 2026; doi:10.1038/s41594-026-01901-9In this Review, the authors summarize structural, biochemical and genetic insights into bacterial immunity, focusing on steps that link infection sensing to activation and effector function.

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ICYMI: New online: Molecular control of bacterial immunity

dlvr.itArchitecture of the Norrin signaling complex and structure-guided surrogate designNature Structural & Molecular Biology, Published online: 21 October 2026; doi:10.1038/s41594-026-01909-1Hu, Li et al. uncover how Norrin assembles Frizzled 4, tetraspanin 12 and low-density lipoprotein receptor-related protein 5 into a signaling complex and use this structural insight to design potent Norrin surrogates, providing a framework for developing therapies for retinal vascular diseases.

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ICYMI: New online: Architecture of the Norrin signaling complex and structure-guided surrogate design

Nature Structural & Molecular Biology reposted

Carolina Perdigoto

@cytochromac.bsky.social

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dlvr.itPhosphorylated M18BP1 activates autoinhibited condensin II to drive mitotic DNA compactionNature Structural & Molecular Biology, Published online: 20 October 2026; doi:10.1038/s41594-026-01910-8By integrating cryo-electron microscopy with single molecule studies, we show that phosphorylated MIS18-binding protein 1 (M18BP1P) relieves condensin II from an autoinhibitory conformation, enabling stable DNA binding and ATP hydrolysis-dependent DNA compaction. In addition, M18BP1–condensin II complex multimers substantially contribute to DNA compaction and might provide mechanical reinforcement of mitotic chromosomes.

ICYMI: New online: Phosphorylated M18BP1 activates autoinhibited condensin II to drive mitotic DNA compaction

dlvr.itMechanism of M18BP1-mediated activation of condensin II for mitotic DNA compactionNature Structural & Molecular Biology, Published online: 20 October 2026; doi:10.1038/s41594-026-01902-8Here, the authors show that phosphorylated M18BP1 activates condensin II by relieving an autoinhibitory interface, enabling stable DNA binding and compaction. Additionally, the M18BP1–condensin II complex forms clusters that might mechanically reinforce mitotic chromosomes.

ICYMI: New online: Mechanism of M18BP1-mediated activation of condensin II for mitotic DNA compaction

dlvr.itMolecular control of bacterial immunityNature Structural & Molecular Biology, Published online: 21 October 2026; doi:10.1038/s41594-026-01901-9In this Review, the authors summarize structural, biochemical and genetic insights into bacterial immunity, focusing on steps that link infection sensing to activation and effector function.

New online: Molecular control of bacterial immunity

dlvr.itArchitecture of the Norrin signaling complex and structure-guided surrogate designNature Structural & Molecular Biology, Published online: 21 October 2026; doi:10.1038/s41594-026-01909-1Hu, Li et al. uncover how Norrin assembles Frizzled 4, tetraspanin 12 and low-density lipoprotein receptor-related protein 5 into a signaling complex and use this structural insight to design potent Norrin surrogates, providing a framework for developing therapies for retinal vascular diseases.

New online: Architecture of the Norrin signaling complex and structure-guided surrogate design

dlvr.itPhosphorylated M18BP1 activates autoinhibited condensin II to drive mitotic DNA compactionNature Structural & Molecular Biology, Published online: 20 October 2026; doi:10.1038/s41594-026-01910-8By integrating cryo-electron microscopy with single molecule studies, we show that phosphorylated MIS18-binding protein 1 (M18BP1P) relieves condensin II from an autoinhibitory conformation, enabling stable DNA binding and ATP hydrolysis-dependent DNA compaction. In addition, M18BP1–condensin II complex multimers substantially contribute to DNA compaction and might provide mechanical reinforcement of mitotic chromosomes.

New online: Phosphorylated M18BP1 activates autoinhibited condensin II to drive mitotic DNA compaction

dlvr.itMechanism of M18BP1-mediated activation of condensin II for mitotic DNA compactionNature Structural & Molecular Biology, Published online: 20 October 2026; doi:10.1038/s41594-026-01902-8Here, the authors show that phosphorylated M18BP1 activates condensin II by relieving an autoinhibitory interface, enabling stable DNA binding and compaction. Additionally, the M18BP1–condensin II complex forms clusters that might mechanically reinforce mitotic chromosomes.

New online: Mechanism of M18BP1-mediated activation of condensin II for mitotic DNA compaction

dlvr.itAlternative splicing fine-tunes modular protein interfaces to control protein localizationNature Structural & Molecular Biology, Published online: 14 October 2026; doi:10.1038/s41594-026-01875-8Kjer-Hansen et al. show that alternative splicing reshapes how proteins interact and where they localize in cells, with tiny microexons making a disproportionate contribution to protein organization and cellular function.

ICYMI: New online: Alternative splicing fine-tunes modular protein interfaces to control protein localization

dlvr.itμ-Opioid ligands tune G-protein opening kineticsNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01861-0There is a thin line between opioids acting to relieve pain and causing life-threatening adverse effects, yet the mechanistic basis separating these outcomes is not fully understood. A study suggests that the difference is encoded in the motions of the G-protein α-helical domain that gates GDP release.

ICYMI: New online: μ-Opioid ligands tune G-protein opening kinetics

dlvr.itLigand-dependent G protein dynamics underlying opioid efficacyNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01893-6Deutsch et al. show how μ-opioid receptor agonists exert long-range allosteric control over bound G proteins, providing an additional mechanism for encoding opioid signaling outcomes.

ICYMI: New online: Ligand-dependent G protein dynamics underlying opioid efficacy

dlvr.itStructural basis of an endoplasmic reticulum EMC:Spf1 insertase–dislocase complexNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01883-8Klose et al. provide structural insights into a supercomplex between the EMC and Spf1 that brings together cellular machines for membrane protein insertion and extraction into a single entity, providing a framework for integrated membrane protein quality control.

ICYMI: New online: Structural basis of an endoplasmic reticulum EMC:Spf1 insertase–dislocase complex

dlvr.itAlternative splicing fine-tunes modular protein interfaces to control protein localizationNature Structural & Molecular Biology, Published online: 14 October 2026; doi:10.1038/s41594-026-01875-8Kjer-Hansen et al. show that alternative splicing reshapes how proteins interact and where they localize in cells, with tiny microexons making a disproportionate contribution to protein organization and cellular function.

New online: Alternative splicing fine-tunes modular protein interfaces to control protein localization

dlvr.itμ-Opioid ligands tune G-protein opening kineticsNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01861-0There is a thin line between opioids acting to relieve pain and causing life-threatening adverse effects, yet the mechanistic basis separating these outcomes is not fully understood. A study suggests that the difference is encoded in the motions of the G-protein α-helical domain that gates GDP release.

New online: μ-Opioid ligands tune G-protein opening kinetics

dlvr.itLigand-dependent G protein dynamics underlying opioid efficacyNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01893-6Deutsch et al. show how μ-opioid receptor agonists exert long-range allosteric control over bound G proteins, providing an additional mechanism for encoding opioid signaling outcomes.

New online: Ligand-dependent G protein dynamics underlying opioid efficacy

dlvr.itStructural basis of an endoplasmic reticulum EMC:Spf1 insertase–dislocase complexNature Structural & Molecular Biology, Published online: 13 October 2026; doi:10.1038/s41594-026-01883-8Klose et al. provide structural insights into a supercomplex between the EMC and Spf1 that brings together cellular machines for membrane protein insertion and extraction into a single entity, providing a framework for integrated membrane protein quality control.

New online: Structural basis of an endoplasmic reticulum EMC:Spf1 insertase–dislocase complex

dlvr.itChill factorNature Structural & Molecular Biology, Published online: 09 October 2026; doi:10.1038/s41594-026-01905-5Chill factor

ICYMI: New online: Chill factor

dlvr.itChill factorNature Structural & Molecular Biology, Published online: 09 October 2026; doi:10.1038/s41594-026-01905-5Chill factor

New online: Chill factor

dlvr.itManipulating rRNA levels with CRISPRNature Structural & Molecular Biology, Published online: 08 October 2026; doi:10.1038/s41594-026-01904-6Manipulating rRNA levels with CRISPR

ICYMI: New online: Manipulating rRNA levels with CRISPR

dlvr.itManipulating rRNA levels with CRISPRNature Structural & Molecular Biology, Published online: 08 October 2026; doi:10.1038/s41594-026-01904-6Manipulating rRNA levels with CRISPR

New online: Manipulating rRNA levels with CRISPR

dlvr.itGlycosylated RNAs travel with extracellular vesicles and shape intercellular communicationNature Structural & Molecular Biology, Published online: 06 October 2026; doi:10.1038/s41594-026-01896-3We describe a proximity-based imaging strategy for tracking glycosylated RNAs (glycoRNAs) on the surface of extracellular vesicles (EVs) and find that vesicle subtypes and cellular states are characterized by distinct glycoRNA signatures. We also demonstrate that in addition to being EV cargo, glycoRNAs contribute to intercellular communication by mediating EV uptake.

ICYMI: New online: Glycosylated RNAs travel with extracellular vesicles and shape intercellular communication

dlvr.itGlycosylated RNAs travel with extracellular vesicles and shape intercellular communicationNature Structural & Molecular Biology, Published online: 06 October 2026; doi:10.1038/s41594-026-01896-3We describe a proximity-based imaging strategy for tracking glycosylated RNAs (glycoRNAs) on the surface of extracellular vesicles (EVs) and find that vesicle subtypes and cellular states are characterized by distinct glycoRNA signatures. We also demonstrate that in addition to being EV cargo, glycoRNAs contribute to intercellular communication by mediating EV uptake.

New online: Glycosylated RNAs travel with extracellular vesicles and shape intercellular communication

dlvr.itSingle-molecule chromatin tracing reveals a diversity of megabase heterochromatin domainsNature Structural & Molecular Biology, Published online: 02 October 2026; doi:10.1038/s41594-026-01895-4Single-molecule imaging reveals diverse, megabase-scale heterochromatin domains in C. elegans. Some resemble TADs and depend on condensin I; others are independent of condensin and histone H3K9me, including one domain that encloses the 5S rDNA locus.

ICYMI: New online: Single-molecule chromatin tracing reveals a diversity of megabase heterochromatin domains

dlvr.itSingle-molecule chromatin tracing reveals a diversity of megabase heterochromatin domainsNature Structural & Molecular Biology, Published online: 02 October 2026; doi:10.1038/s41594-026-01895-4Single-molecule imaging reveals diverse, megabase-scale heterochromatin domains in C. elegans. Some resemble TADs and depend on condensin I; others are independent of condensin and histone H3K9me, including one domain that encloses the 5S rDNA locus.

New online: Single-molecule chromatin tracing reveals a diversity of megabase heterochromatin domains

dlvr.itMapping functional signaling landscapes across the human phosphoproteomeNature Structural & Molecular Biology, Published online: 30 September 2026; doi:10.1038/s41594-026-01898-1Advances in phosphoproteomics enable systems-wide mapping of phosphorylation, but translating these data into functional signaling networks remains challenging. A deep human cell-line phosphoproteome atlas infers kinase activity, enabling systematic network mapping and identification of actionable kinase vulnerabilities for precision therapies.

ICYMI: New online: Mapping functional signaling landscapes across the human phosphoproteome

dlvr.itA phosphoproteome atlas of human cell lines reveals the landscape of kinase activityNature Structural & Molecular Biology, Published online: 30 September 2026; doi:10.1038/s41594-026-01877-6Koenig et al. present a phosphoproteome atlas of 33 human cell lines covering >200,000 phosphosites, advancing cellular kinase activity scoring and drug sensitivity prediction, providing a resource for cell signaling insights and precision oncology.

ICYMI: New online: A phosphoproteome atlas of human cell lines reveals the landscape of kinase activity

dlvr.itMapping functional signaling landscapes across the human phosphoproteomeNature Structural & Molecular Biology, Published online: 30 September 2026; doi:10.1038/s41594-026-01898-1Advances in phosphoproteomics enable systems-wide mapping of phosphorylation, but translating these data into functional signaling networks remains challenging. A deep human cell-line phosphoproteome atlas infers kinase activity, enabling systematic network mapping and identification of actionable kinase vulnerabilities for precision therapies.

New online: Mapping functional signaling landscapes across the human phosphoproteome

dlvr.itA phosphoproteome atlas of human cell lines reveals the landscape of kinase activityNature Structural & Molecular Biology, Published online: 30 September 2026; doi:10.1038/s41594-026-01877-6Koenig et al. present a phosphoproteome atlas of 33 human cell lines covering >200,000 phosphosites, advancing cellular kinase activity scoring and drug sensitivity prediction, providing a resource for cell signaling insights and precision oncology.

New online: A phosphoproteome atlas of human cell lines reveals the landscape of kinase activity

dlvr.itMechanical regulation of cell memoryNature Structural & Molecular Biology, Published online: 29 September 2026; doi:10.1038/s41594-026-01886-5In this Review, Wu, Rashid et al. discuss how mechanical signals regulate the ability of cells to facilitate and maintain changes in cell memory. They exemplify these effects in cellular structure remodeling and epigenetic regulation.

ICYMI: New online: Mechanical regulation of cell memory

dlvr.itMechanical regulation of cell memoryNature Structural & Molecular Biology, Published online: 29 September 2026; doi:10.1038/s41594-026-01886-5In this Review, Wu, Rashid et al. discuss how mechanical signals regulate the ability of cells to facilitate and maintain changes in cell memory. They exemplify these effects in cellular structure remodeling and epigenetic regulation.

New online: Mechanical regulation of cell memory

dlvr.itCotranslational membrane protein biogenesis by an EMC-bound transloconNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01889-2The authors use selective ribosome profiling, cryo-ET and site-specific photocrosslinking to show how the ER membrane protein complex (EMC) cooperates with ribosome-bound translocons to facilitate multipass membrane protein biogenesis in human cells.

ICYMI: New online: Cotranslational membrane protein biogenesis by an EMC-bound translocon

dlvr.itProfiling extracellular vesicle glycoRNAs defines their function in vesicular communicationNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01897-2The authors expand the extracellular vesicle glycosylated RNA (glycoRNA) landscape and reveal distinct glycoRNA profiles across extracellular vesicle (EV) subtypes, cell types and passage numbers. They also show that glycoRNAs are not only EV cargoes but also regulators of EV uptake, uncovering a layer of vesicle-mediated communication.

ICYMI: New online: Profiling extracellular vesicle glycoRNAs defines their function in vesicular communication

dlvr.itHERC4-mediated ubiquitination licenses RIPK1 to initiate TNF-induced cell deathNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01871-yLu and Du et al. show that HERC4 E3 ligase ubiquitinates S166-phosphorylated RIPK1 to initiate prodeath complex assembly and TNF-induced cell death, acting as the pivotal prodeath switch and that loss of HERC4 protects mice from TNF-driven inflammation and liver injury.

ICYMI: New online: HERC4-mediated ubiquitination licenses RIPK1 to initiate TNF-induced cell death

dlvr.itCotranslational membrane protein biogenesis by an EMC-bound transloconNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01889-2The authors use selective ribosome profiling, cryo-ET and site-specific photocrosslinking to show how the ER membrane protein complex (EMC) cooperates with ribosome-bound translocons to facilitate multipass membrane protein biogenesis in human cells.

New online: Cotranslational membrane protein biogenesis by an EMC-bound translocon

dlvr.itProfiling extracellular vesicle glycoRNAs defines their function in vesicular communicationNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01897-2The authors expand the extracellular vesicle glycosylated RNA (glycoRNA) landscape and reveal distinct glycoRNA profiles across extracellular vesicle (EV) subtypes, cell types and passage numbers. They also show that glycoRNAs are not only EV cargoes but also regulators of EV uptake, uncovering a layer of vesicle-mediated communication.

New online: Profiling extracellular vesicle glycoRNAs defines their function in vesicular communication

dlvr.itHERC4-mediated ubiquitination licenses RIPK1 to initiate TNF-induced cell deathNature Structural & Molecular Biology, Published online: 28 September 2026; doi:10.1038/s41594-026-01871-yLu and Du et al. show that HERC4 E3 ligase ubiquitinates S166-phosphorylated RIPK1 to initiate prodeath complex assembly and TNF-induced cell death, acting as the pivotal prodeath switch and that loss of HERC4 protects mice from TNF-driven inflammation and liver injury.

New online: HERC4-mediated ubiquitination licenses RIPK1 to initiate TNF-induced cell death

dlvr.itSculpting semisynthetic conducting protein pores by de novo designNature Structural & Molecular Biology, Published online: 22 September 2026; doi:10.1038/s41594-026-01880-xThe lumen geometry and chemistry of a protein nanopore govern its ion-conduction properties. Rather than redesigning an entire pore assembly, or mutating a naturally occurring pore, we built on the bacterial CsgG nanopore scaffold with an integral de novo component, which yielded semisynthetic conducting pores with programmed architecture and distinct ion-conduction profiles, including rectifying behavior.

ICYMI: New online: Sculpting semisynthetic conducting protein pores by de novo design

dlvr.itSculpting semisynthetic conducting protein pores by de novo designNature Structural & Molecular Biology, Published online: 22 September 2026; doi:10.1038/s41594-026-01880-xThe lumen geometry and chemistry of a protein nanopore govern its ion-conduction properties. Rather than redesigning an entire pore assembly, or mutating a naturally occurring pore, we built on the bacterial CsgG nanopore scaffold with an integral de novo component, which yielded semisynthetic conducting pores with programmed architecture and distinct ion-conduction profiles, including rectifying behavior.

22 Sept

New online: Sculpting semisynthetic conducting protein pores by de novo design

dlvr.itDe novo design of semisynthetic conduction poresNature Structural & Molecular Biology, Published online: 21 September 2026; doi:10.1038/s41594-026-01881-wSchnaider et al. develop a protein design strategy for building a new component within a confined, symmetric pore. Cryo-EM confirms the designed lumen architecture, while electrical recordings reveal distinct and tunable current rectification.

22 Sept

ICYMI: New online: De novo design of semisynthetic conduction pores

dlvr.itDe novo design of semisynthetic conduction poresNature Structural & Molecular Biology, Published online: 21 September 2026; doi:10.1038/s41594-026-01881-wSchnaider et al. develop a protein design strategy for building a new component within a confined, symmetric pore. Cryo-EM confirms the designed lumen architecture, while electrical recordings reveal distinct and tunable current rectification.

21 Sept

New online: De novo design of semisynthetic conduction pores

dlvr.itCapturing ATR–ATRIP in the act of activationNature Structural & Molecular Biology, Published online: 17 September 2026; doi:10.1038/s41594-026-01899-0The ATR–ATRIP kinase complex safeguards genome integrity by coordinating cellular responses to DNA damage and replication stress. Two recent cryo-EM studies resolve the structural basis of ATR–ATRIP activation, capturing distinct active states of the kinase and clarifying how its activity is stimulated by TOPBP1 and ETAA1.

18 Sept

ICYMI: New online: Capturing ATR–ATRIP in the act of activation

dlvr.itMechanistic insights into phosphorylation-driven activation and therapeutic inhibition of human ATR–ATRIPNature Structural & Molecular Biology, Published online: 17 September 2026; doi:10.1038/s41594-026-01887-4Wang et al. present cryo-electron microscopy structures of ATR–ATRIP complexes in distinct functional states, revealing ATP-dependent and TopBP1-dependent mechanisms of kinase activation and how ATR inhibitors exploit ATP-binding pocket flexibility for selective inhibition.

18 Sept

ICYMI: New online: Mechanistic insights into phosphorylation-driven activation and therapeutic inhibition of human ATR–ATRIP

dlvr.itStructure-guided discovery and engineering of miniature CRISPR–Cas12m for epigenome editingNature Structural & Molecular Biology, Published online: 16 September 2026; doi:10.1038/s41594-026-01890-9The authors identified and engineered a miniature, innate nuclease-dead xCas12m enabling effective epigenome editing. xCas12m–CRISPRoff achieved durable epigenetic silencing and inhibition of hepatitis B virus infection through single-AAV delivery.

17 Sept

ICYMI: New online: Structure-guided discovery and engineering of miniature CRISPR–Cas12m for epigenome editing

dlvr.itCapturing ATR–ATRIP in the act of activationNature Structural & Molecular Biology, Published online: 17 September 2026; doi:10.1038/s41594-026-01899-0The ATR–ATRIP kinase complex safeguards genome integrity by coordinating cellular responses to DNA damage and replication stress. Two recent cryo-EM studies resolve the structural basis of ATR–ATRIP activation, capturing distinct active states of the kinase and clarifying how its activity is stimulated by TOPBP1 and ETAA1.

17 Sept

New online: Capturing ATR–ATRIP in the act of activation

dlvr.itMechanistic insights into phosphorylation-driven activation and therapeutic inhibition of human ATR–ATRIPNature Structural & Molecular Biology, Published online: 17 September 2026; doi:10.1038/s41594-026-01887-4Wang et al. present cryo-electron microscopy structures of ATR–ATRIP complexes in distinct functional states, revealing ATP-dependent and TopBP1-dependent mechanisms of kinase activation and how ATR inhibitors exploit ATP-binding pocket flexibility for selective inhibition.

17 Sept

New online: Mechanistic insights into phosphorylation-driven activation and therapeutic inhibition of human ATR–ATRIP

dlvr.itStructure-guided discovery and engineering of miniature CRISPR–Cas12m for epigenome editingNature Structural & Molecular Biology, Published online: 16 September 2026; doi:10.1038/s41594-026-01890-9The authors identified and engineered a miniature, innate nuclease-dead xCas12m enabling effective epigenome editing. xCas12m–CRISPRoff achieved durable epigenetic silencing and inhibition of hepatitis B virus infection through single-AAV delivery.

16 Sept

New online: Structure-guided discovery and engineering of miniature CRISPR–Cas12m for epigenome editing

dlvr.itCryo-EM structure, enzymatic activity and genome targeting of canonical PRC1Nature Structural & Molecular Biology, Published online: 14 September 2026; doi:10.1038/s41594-026-01885-6Ciapponi et al. determine the cryo-electron microscopy structure of the canonical Polycomb repressive complex 1 holocomplex and show how its architecture coordinates complex assembly, H2A monoubiquitination and genomic targeting.

15 Sept

ICYMI: New online: Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1