Cited by 13

The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.

Explosion in the complexity of membrane protein recycling

McDonald, Fiona J.·2021·American Journal of Physiology-Cell Physiology

Abstract

For decades, recycling of membrane proteins has been represented in figures by arrows between the “endosome” and the plasma membrane, but recently there has been an explosion in the understanding of the mechanisms and protein complexes required to facilitate protein recycling. Here, some key discoveries will be introduced, including assigning function to a number of recently recognized protein complexes and linking their function to protein recycling. Furthermore, the importance of lipid interactions and links to diseases and epithelial polarity will be summarized.

Overview

Integrity signals

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Crossref · 10.1152/ajpcell.00171.2020

Cites

12 of 12 references verified0 citation errors · 0 not checkable

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  • Recycling of internalized membrane proteins back to the cell surface is achieved by at least two distinct pathways, the SNX27-Retromer and SNX17-Retriever pathways.

    “In recent years, it has become clear that recycling of internalized membrane proteins back to the cell surface is achieved by at least 2 distinct pathways – the SNX27-Retromer and SNX17-Retriever pathways (McNally et al., 2017; Chen et al., 2019; McDonald, 2020).”
  • Disruptions in protein recycling impair synaptic plasticity and have been linked to neurodevelopmental and neurodegenerative disorders.

    “Disruptions in protein recycling impair synaptic plasticity and have been linked to neurodevelopmental and neurodegenerative disorders”

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Metadata

Authors
McDonald, F. J.
Affiliations
Department of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand
Venue
American Journal of Physiology-Cell Physiology
Published
2021-04-01
Volume
320
Issue
4
Pages
C483-C494
ISSN
  • 0363-6143
  • 1522-1563
Cited by
13
References
12
Language
en
Funders
  • Lottery Health New Zealand (LHR-2016-26783)
  • University of Otago Research Grant (2015, 2013)
  • Department of Physiology, University of Otago
  • Royal Society of New Zealand | Marsden Fund (U00-04-01, 02_UOA_128)

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