7BLN

VPS35/VPS29 arch of metazoan membrane-assembled retromer:SNX3 complex modelled with human proteins

Summary for 7BLN

• Entry DOI: 10.2210/pdb7bln/pdb
• Related: 7BLO
• EMDB information: 12220 12221 12222
• Descriptor: Vacuolar protein sorting-associated protein 29, Vacuolar protein sorting-associated protein 35 (2 entities in total)
• Functional Keywords: endosomes, coat proteins, membrane trafficking, cargo-sorting, endocytosis
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 224697.02

Authors

Leneva, N.,Kovtun, O.,Morado, D.R.,Briggs, J.A.G.,Owen, D.J. (deposition date: 2021-01-18, release date: 2021-02-10, Last modification date: 2024-05-01)

Primary citation

Leneva, N.,Kovtun, O.,Morado, D.R.,Briggs, J.A.G.,Owen, D.J.
Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly.
Sci Adv, 7:-, 2021

PubMed Abstract: Retromer is a master regulator of cargo retrieval from endosomes, which is critical for many cellular processes including signaling, immunity, neuroprotection, and virus infection. The retromer core (VPS26/VPS29/VPS35) is present on cargo-transporting, tubular carriers along with a range of sorting nexins. Here, we elucidate the structural basis of membrane tubulation and coupled cargo recognition by metazoan and fungal retromer coats assembled with the non-Bin1/Amphiphysin/Rvs (BAR) sorting nexin SNX3 using cryo-electron tomography. The retromer core retains its arched, scaffolding structure but changes its mode of membrane recruitment when assembled with different SNX adaptors, allowing cargo recognition at subunit interfaces. Thus, membrane bending and cargo incorporation can be modulated to allow retromer to traffic cargoes along different cellular transport routes.

PubMed: 33762348
DOI: 10.1126/sciadv.abf8598

Experimental method

ELECTRON MICROSCOPY (8.9 Å)