8P0X

Structure of the human Commander complex Retriever Subcomplex

This is a non-PDB format compatible entry.

Summary for 8P0X

• Entry DOI: 10.2210/pdb8p0x/pdb
• EMDB information: 17341
• Descriptor: Coiled-coil domain-containing protein 93, Coiled-coil domain-containing protein 22, Vacuolar protein sorting-associated protein 29, ... (5 entities in total)
• Functional Keywords: alpha solenoid, arrestin fold, phosphoesterase fold, complex, unknown function
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 307457.79

Authors

Kumpula, E.P.,Laulumaa, S.,Huiskonen, J.T. (deposition date: 2023-05-11, release date: 2024-03-20, Last modification date: 2024-07-03)

Primary citation

Laulumaa, S.,Kumpula, E.P.,Huiskonen, J.T.,Varjosalo, M.
Structure and interactions of the endogenous human Commander complex.
Nat.Struct.Mol.Biol., 31:925-938, 2024

PubMed Abstract: The Commander complex, a 16-protein assembly, plays multiple roles in cell homeostasis, cell cycle and immune response. It consists of copper-metabolism Murr1 domain proteins (COMMD1-10), coiled-coil domain-containing proteins (CCDC22 and CCDC93), DENND10 and the Retriever subcomplex (VPS26C, VPS29 and VPS35L), all expressed ubiquitously in the body and linked to various diseases. Here, we report the structure and key interactions of the endogenous human Commander complex by cryogenic-electron microscopy and mass spectrometry-based proteomics. The complex consists of a stable core of COMMD1-10 and an effector containing DENND10 and Retriever, scaffolded together by CCDC22 and CCDC93. We establish the composition of Commander and reveal major interaction interfaces. These findings clarify its roles in intracellular transport, and uncover a strong association with cilium assembly, and centrosome and centriole functions.

PubMed: 38459129
DOI: 10.1038/s41594-024-01246-1

Experimental method

ELECTRON MICROSCOPY (7.5 Å)