Cited by 39Cellular transport and secretionCaveolin-1 and cellular processesAutophagy in Disease and Therapy

Clathrin’s life beyond 40: Connecting biochemistry with physiology and disease

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Briant, Kit, Redlingshöfer, Lisa, Brodsky, Frances M.·2020·Current Opinion in Cell Biology

Abstract

Understanding of the range and mechanisms of clathrin functions has developed exponentially since clathrin's discovery in 1975. Here, newly established molecular mechanisms that regulate clathrin activity and connect clathrin pathways to differentiation, disease and physiological processes such as glucose metabolism are reviewed. Diversity and commonalities of clathrin pathways across the tree of life reveal species-specific differences enabling functional plasticity in both membrane traffic and cytokinesis. New structural information on clathrin coat formation and cargo interactions emphasises the interplay between clathrin, adaptor proteins, lipids and cargo, and how this interplay regulates quality control of clathrin's function and is compromised in infection and neurological disease. Roles for balancing clathrin-mediated cargo transport are defined in stem cell development and additional disease states.

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Crossref · 10.1016/j.ceb.2020.06.004

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  • CME requires the AP2 complex to recruit cargo proteins to endocytic vesicles.

    “To recruit cargo proteins to endocytic vesicles, CME requires the heterotetrameric adaptor protein complex AP2 complex that acts as an adaptor between cargo proteins and clathrin coats (5, 15–18).”

    From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [5]

    In “Phylogenetic and population diversity” (page unavailable), the review identifies AP2 as a tetrameric adaptor associated with clathrin at the plasma membrane and describes cargo binding to AP2. Its “Cargo transport pathways” section also describes ankyrin B as an adaptor for GLUT4 uptake by CME. The source therefore supports AP2’s adaptor role, but not the unqualified claim that CME requires AP2 to recruit cargo. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • Surface levels of membrane proteins are determined by the dynamic balance of exocytosis-mediated delivery and endocytosis-dependent retrieval.

    “The surface level of a protein is determined by the dynamic balance of its delivery to the plasma membrane through exocytic pathways (including recycling exocytosis) and removal from the plasma membrane by endocytic pathways (4–6).”

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Cited by

Sorted by citations

Authors
Briant, K., Redlingshöfer, L., & Brodsky, F. M.
Affiliations
Institute of Structural and Molecular Biology (GB)
Corresponding author
Brodsky, Frances M.
Venue
Current Opinion in Cell Biology
Publisher
Elsevier BV
Published
2020-08
Volume
65
Pages
141-149
ISSN
0955-0674 (ISSN-L)
OpenAlex
W3081368827
Cited by
39
References
0
Citations by year
2026: 5 · 2025: 6 · 2024: 5 · 2023: 7 · 2022: 7 · 2021: 8 · 2020: 1
FWCI
0.69
Type
journal article
Language
en
Open access
Locations
  • Current Opinion in Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
  • Medical Research Council
  • Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
clathrin, clathrin-mediated endocytosis, adaptor proteins, cargo binding, membrane traffic, cytokinesis, glucose metabolism, cell differentiation, stem cell development, neurological disorders, infection
MeSH terms
Animals, Biological Transport, Clathrin, Disease, Humans, Models, Biological, Organ Specificity, Phylogeny

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