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5VNE

Crystal structure of Sec23a/Sec24a/Sec22 complexed with Emp24 sorting motif

Summary for 5VNE
Entry DOI10.2210/pdb5vne/pdb
Related5VNF 5VNG 5VNH 5VNI 5VNJ 5VNK 5VNL 5VNM 5VNN 5VNO
DescriptorProtein transport protein Sec23A, Protein transport protein Sec24A, Vesicle-trafficking protein SEC22b, ... (6 entities in total)
Functional Keywordscopii, trafficking, emp24, er retention, protein transport
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : Q15436 O95486
Endoplasmic reticulum membrane ; Single-pass type IV membrane protein : O08547
Total number of polymer chains4
Total formula weight188995.08
Authors
Ma, W.,Goldberg, J. (deposition date: 2017-04-30, release date: 2017-07-05, Last modification date: 2023-10-04)
Primary citationMa, W.,Goldberg, E.,Goldberg, J.
ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Elife, 6:-, 2017
Cited by
PubMed Abstract: Native cargo proteins exit the endoplasmic reticulum (ER) in COPII-coated vesicles, whereas resident and misfolded proteins are substantially excluded from vesicles by a retention mechanism that remains unresolved. We probed the ER retention process using the proteostasis regulator 4-phenylbutyrate (4-PBA), which we show targets COPII protein to reduce the stringency of retention. 4-PBA competes with p24 proteins to bind COPII. When p24 protein uptake is blocked, COPII vesicles package resident proteins and an ER-trapped mutant LDL receptor. We further show that 4-PBA triggers the secretion of a KDEL-tagged luminal resident, implying that a compromised retention mechanism causes saturation of the KDEL retrieval system. The results indicate that stringent ER retention requires the COPII coat machinery to actively sort biosynthetic cargo from diffusible misfolded and resident ER proteins.
PubMed: 28594326
DOI: 10.7554/eLife.26624
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.698 Å)
Structure validation

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