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Assembly and Solution Structure of the Core Retromer Protein Complex
Abstract
Retromer is a peripheral membrane protein complex that has pleiotropic roles in endosomal membrane trafficking. The core of retromer possesses three subunits, VPS35, VPS29 and VPS26, that play different roles in binding to cargo, regulatory proteins and complex stabilization. We have performed an investigation of the thermodynamics of core retromer assembly using isothermal titration calorimetry (ITC) demonstrating that VPS35 acts as the central subunit to which VPS29 and VPS26 bind independently. Furthermore, we confirm that the conserved PRLYL motif of the large VPS35 subunit is critical for direct VPS26 interaction. Heat capacity measurements of VPS29 and VPS26 binding to VPS35 indicate extensive binding interfaces and suggest conformational alterations in VPS29 or VPS35 upon complex formation. Solution studies of the retromer core using small‐angle X‐ray scattering allow us to propose a model whereby VPS35 forms an extended platform with VPS29 and VPS26 bound at distal ends, with the potential for forming dimeric assemblies.
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The metazoan equivalent assembly has evolved into two functionally distinct complexes, the retromer (VPS26-VPS35-VPS29) and the ESCPE-1 (SNX1/SNX2 and SNX5/SNX6) complexes.
“An increasing body of biochemical, cellular and in vivo functional data are consistent with the equivalent metazoan assembly having evolved into two functionally distinct complexes, the retromer (VPS26–VPS35–VPS29) and the ESCPE-1 (SNX1/SNX2 and SNX5/SNX6) complexes (Norwood et al., 2011; Swarbrick et al., 2011; Kvainickas et al., 2017; Simonetti et al., 2017, 2019; Strutt et al., 2019).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Norwood et al., 2011
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Retromer: A Master Conductor of Endosome Sorting
Burd, C., & Cullen, P. J. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016774 · Cited by 435
Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3610 · Cited by 346
Self-citationEndosomal retrieval of cargo: Retromer is not alone
McNally, K. E., & Cullen, P. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.005 · Cited by 169
Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome
Healy, M. D., McNally, K. E., Butkovič, R., Chilton, M., Kato, K., Sacharz, J., McConville, C., Moody, E. R. R., Shaw, S., Planelles-Herrero, V. J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.04.003 · Cited by 91
Self-citationReceptor Recycling by Retromer
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2023) · Molecular and Cellular Biology · doi:10.1080/10985549.2023.2222053 · Cited by 36
Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting
Evans, A. J., Daly, J. L., Anuar, A. N. K., Simonetti, B., & Cullen, P. J. (2020) · Journal of Cell Science · doi:10.1242/jcs.246033 · Cited by 25
Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation
Antón-Plágaro, C., Chen, K.-E., Guo, Q., Liu, M., Evans, A. J., Lewis, P. A., Heesom, K. J., Wilkinson, K. A., Collins, B. M., & Cullen, P. J. (2025) · Nature Communications · doi:10.1038/s41467-025-61802-1 · Cited by 14
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Metadata
- Authors
- Norwood, S. J., Shaw, D. J., Cowieson, N. P., Owen, D. J., Teasdale, R. D., & Collins, B. M.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2010-10-15
- Volume
- 12
- Issue
- 1
- Pages
- 56-71
- ISSN
- 1398-9219
- 1600-0854
- Cited by
- 84
- References
- 1
- Language
- en
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