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8XFB

Cryo-EM structure of partial dimeric WDR11-FAM91A1 complex

Summary for 8XFB
Entry DOI10.2210/pdb8xfb/pdb
EMDB information38300
DescriptorWD repeat-containing protein 11, Protein FAM91A1 (2 entities in total)
Functional Keywordscryo-em, vesicle trafficking, neural development, protein transport
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight368940.05
Authors
Jia, G.W.,Deng, Q.H.,Su, Z.M.,Jia, D. (deposition date: 2023-12-13, release date: 2024-08-14, Last modification date: 2024-10-09)
Primary citationDeng, H.,Jia, G.,Li, P.,Tang, Y.,Zhao, L.,Yang, Q.,Zhao, J.,Wang, J.,Tu, Y.,Yong, X.,Zhang, S.,Mo, X.,Billadeau, D.D.,Su, Z.,Jia, D.
The WDR11 complex is a receptor for acidic-cluster-containing cargo proteins.
Cell, 187:4272-, 2024
Cited by
PubMed Abstract: Vesicle trafficking is a fundamental process that allows for the sorting and transport of specific proteins (i.e., "cargoes") to different compartments of eukaryotic cells. Cargo recognition primarily occurs through coats and the associated proteins at the donor membrane. However, it remains unclear whether cargoes can also be selected at other stages of vesicle trafficking to further enhance the fidelity of the process. The WDR11-FAM91A1 complex functions downstream of the clathrin-associated AP-1 complex to facilitate protein transport from endosomes to the TGN. Here, we report the cryo-EM structure of human WDR11-FAM91A1 complex. WDR11 directly and specifically recognizes a subset of acidic clusters, which we term super acidic clusters (SACs). WDR11 complex assembly and its binding to SAC-containing proteins are indispensable for the trafficking of SAC-containing proteins and proper neuronal development in zebrafish. Our studies thus uncover that cargo proteins could be recognized in a sequence-specific manner downstream of a protein coat.
PubMed: 39013469
DOI: 10.1016/j.cell.2024.06.024
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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