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Cited by 286

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Functional architecture of the retromer cargo-recognition complex

Hierro, Aitor, Rojas, Adriana L., Rojas, Raul, Murthy, Namita, Effantin, Grégory, Kajava, Andrey V., Steven, Alasdair C., Bonifacino, Juan S., Hurley, James H.·2007·Nature
DOI 10.1038/nature06216
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Crossref · 10.1038/nature06216

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  • CCDC22, CCDC93, and seven COMMDs form the CCC complex, which is required for endosomal recycling of certain cargos including copper transporters, Notch family members and LDLR.

    “These form the CCC complex39, shown to be required for the endosomal recycling of certain cargos, including copper transporters39, Notch family members39, 40 and LDLR41.”

    From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [41]

    The Abstract describes the retromer complex and its Vps26, Vps29, Vps35, and SNX subunits, not the CCC complex. Searches for CCDC22, CCDC93, COMMDs, copper transporters, Notch, and LDLR found no passage addressing the attributed CCC composition or recycling functions. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

  • VPS35L is an extended α-solenoid that binds VPS26C and VPS29 at its amino- and carboxy-terminal ends respectively.

    “Analogous to Retromer,57,58,59,60,61,62 VPS35L is an extended α-solenoid that binds VPS26C and VPS29 at its amino- and carboxy-terminal ends respectively (Figures 1B and S1A).”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [57]

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Citations

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Research works printed but not linked: 44

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  11. Strochlic, T. I., Setty, T. G., Sitaram, A. & Burd, C. G. Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. J. Cell Biol. 177, 115–125 (2007) · DOI · Paper page
  12. Small, S. A. et al. Model-guided microarray implicates the retromer complex in Alzheimer’s disease. Ann. Neurol. 58, 909–919 (2005) · DOI · Paper page
  13. Rojas, R., Kametaka, S., Haft, C. R. & Bonifacino, J. S. Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of the mannose 6-phosphate receptors. Mol. Cell. Biol. 27, 1112–1124 (2007) · DOI
  14. Wang, D. et al. Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. J. Biol. Chem. 280, 22962–22967 (2005) · DOI
  15. Collins, B. M., Skinner, C. F., Watson, P. J., Seaman, M. N. & Owen, D. J. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly. Nature Struct. Mol. Biol. 12, 594–602 (2005) · DOI
  16. Shi, H., Rojas, R., Bonifacino, J. S. & Hurley, J. H. The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain. Nature Struct. Mol. Biol. 13, 540–548 (2006) · DOI
  17. Damen, E., Krieger, E., Nielsen, J. E., Eygensteyn, J. & van Leeuwen, J. E. M. The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide. Biochem. J. 398, 399–409 (2006) · DOI
  18. Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R. & Owen, D. J. Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523–535 (2002) · DOI · Paper page
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Metadata

Authors
Hierro, A., Rojas, A. L., Rojas, R., Murthy, N., Effantin, G., Kajava, A. V., Steven, A. C., Bonifacino, J. S., & Hurley, J. H.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2007-09-23
Volume
449
Issue
7165
Pages
1063-1067
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature06216
Cited by
286
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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