[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleAtomic mechanisms of full-length ASC-mediated inflammasome assembly.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10564, Year 2025
Publish dateNov 26, 2025
AuthorsDongmei Xue / Fengyun Ni / Sheng Liu / Huifang Yan / Zhenwei Luo / Gang Fu / Qinghua Wang / Jianpeng Ma /
PubMed AbstractASC (Apoptosis-associated Speck-like protein containing a CARD) is a key adaptor protein that assembles inflammasomes by linking sensors such as NLRP3 to effectors like Caspase-1 via its PYD and CARD ...ASC (Apoptosis-associated Speck-like protein containing a CARD) is a key adaptor protein that assembles inflammasomes by linking sensors such as NLRP3 to effectors like Caspase-1 via its PYD and CARD Death Domains. Due to ASC's propensity to self-aggregate, most high-resolution structural studies focused on isolated PYD or CARD domains, leaving the atomic basis of full-length ASC assembly unknown. Here we determine atomic-resolution cryo-EM structures of PYD and CARD filaments from full-length ASC, revealing characteristic multitrack bundles composed of alternating ASC and ASC filaments that expose multiple interfaces for flexible assembly and efficient signaling. We further show that Caspase-1 filaments nucleate specifically from the B-end of ASC filaments, and that the interdomain linker modulates bundle formation. The ASC isoform ASCb, with a four-residue linker, adopts a distinct architecture, correlating with reduced Caspase-1 activation efficiency. In ASC THP-1 cells, only wild-type ASC, not interface-disrupting mutants, restored ASC speck formation and Caspase-1 activation, underscoring the requirement for intact multitrack bundles. Cryo-electron tomography captures snapshots of higher-order inflammasome structures. These findings collectively define the structural and functional principles by which ASC organizes inflammasomes to amplify immune signaling.
External linksNat Commun / PubMed:41298390 / PubMed Central
MethodsEM (helical sym.)
Resolution2.45 - 4.41 Å
Structure data

66381

9wz4

EMDB-66381, PDB-9wz4:
Full-length ASC-PYD filament
Method: EM (helical sym.) / Resolution: 3.21 Å

66382

9wz5

EMDB-66382, PDB-9wz5:
Full-length ASC-CARD filament
Method: EM (helical sym.) / Resolution: 2.91 Å

66383

9wz6

EMDB-66383, PDB-9wz6:
Full-length Caspase-1-CARD filament
Method: EM (helical sym.) / Resolution: 2.66 Å

66384

9wz7

EMDB-66384, PDB-9wz7:
Full-length ASCb filament
Method: EM (helical sym.) / Resolution: 2.66 Å

66385

9wz8

EMDB-66385, PDB-9wz8:
Full-length ASC-GFP PYD-filament
Method: EM (helical sym.) / Resolution: 3.14 Å

66387

9wzb

EMDB-66387, PDB-9wzb:
K21E/K22E-ASC CARD filament
Method: EM (helical sym.) / Resolution: 2.67 Å

66388

9wzc

EMDB-66388, PDB-9wzc:
R41E-ASC CARD filament
Method: EM (helical sym.) / Resolution: 2.45 Å

66391

9wzd

EMDB-66391, PDB-9wzd:
R125E-ASC PYD filament
Method: EM (helical sym.) / Resolution: 2.86 Å

66401

9wzg

EMDB-66401, PDB-9wzg:
Full-length ASC-PYD filament
Method: EM (helical sym.) / Resolution: 4.41 Å

66402

9wzh

EMDB-66402, PDB-9wzh:
Full-length ASC-CARD filament
Method: EM (helical sym.) / Resolution: 4.02 Å

66403

9wzi

EMDB-66403, PDB-9wzi:
Full-length Caspase-1-CARD filament
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / filament / PYD / CARD

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more