Retro Is Cool: Structure of the Versatile Retromer Complex

Leonora Martínez-Núñez; Mary Munson

doi:10.1016/j.str.2020.03.009

Retro Is Cool: Structure of the Versatile Retromer Complex

Structure. 2020 Apr 7;28(4):387-389. doi: 10.1016/j.str.2020.03.009.

Authors

Leonora Martínez-Núñez¹, Mary Munson²

Affiliations

¹ Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA.
² Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA. Electronic address: mary.munson@umassmed.edu.

PMID: 32268076
DOI: 10.1016/j.str.2020.03.009

Abstract

In this issue of Structure, Kendall et al. (2020) reveal the cryo-EM structure of the mammalian retromer complex, which is essential in sorting membrane proteins in endosomes. The retromer heterotrimer can oligomerize in multiple conformations; this versatility is promoted by a flexible interface of electrostatic residues on the VPS35 subunit.

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MeSH terms

Animals
Endosomes*
Membrane Proteins
Protein Transport
Vesicular Transport Proteins*

Substances

Membrane Proteins
Vesicular Transport Proteins