[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

TitleMolecular mechanism of dynein-dynactin complex assembly by LIS1.
Journal, issue, pagesScience, Vol. 383, Issue 6690, Page eadk8544, Year 2024
Publish dateMar 29, 2024
AuthorsKashish Singh / Clinton K Lau / Giulia Manigrasso / José B Gama / Reto Gassmann / Andrew P Carter /
PubMed AbstractCytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil ...Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation.
External linksScience / PubMed:38547289 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 10.0 Å
Structure data

EMDB-17825, PDB-8pqv:
Cytoplasmic dynein-1 motor domain in post-powerstroke state
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-17826, PDB-8pqw:
Cytoplasmic dynein-1 motor domain bound to dynactin-p150glued and LIS1
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-17828, PDB-8pqy:
Cytoplasmic dynein-1 motor domain bound to LIS1
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-17829, PDB-8pqz:
Cytoplasmic dynein-1 A1/A2 motor domains bound to LIS1
Method: EM (single particle) / Resolution: 5.5 Å

EMDB-17830, PDB-8pr0:
Cytoplasmic dynein-A heavy chain bound to dynactin-p150glued and IC-LC tower
Method: EM (single particle) / Resolution: 9.4 Å

EMDB-17831, PDB-8pr1:
Cytoplasmic dynein-B heavy chain bound to IC-LC tower
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-17832, PDB-8pr2:
Cytoplasmic dynein-1 heavy chain bound to JIP3-LZI
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-17833, PDB-8pr3:
Cytoplasmic dynein-1 heavy chain bound to JIP3-RH1
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-17834, PDB-8pr4:
Dynactin pointed end bound to JIP3
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-17835: Consensus cryo-EM structure of Dynein-Dynactin-JIP3(1-185)-LIS1
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-17836: Consensus cryo-EM structure of Dynein-dynactin-JIP3(1-560)-LIS1
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-17873, PDB-8ptk:
Composite structure of Dynein-Dynactin-JIP3-LIS1
Method: EM (single particle) / Resolution: 10.0 Å

PDB-8pr5:
Structure of the autoinhibited dynactin p150glued projection
Method: ELECTRON MICROSCOPY / Resolution: 8.6 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
  • sus scrofa (pig)
KeywordsMOTOR PROTEIN / Dynein / AAA-Atpase / p150 / LIS1 / dynactin / LC8 / TCTEX1 / JIP3

+
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