CALM supports clathrin-coated vesicle completion upon membrane tension increase.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
22 06 2021
Historique:
entrez: 22 6 2021
pubmed: 23 6 2021
medline: 15 12 2021
Statut: ppublish

Résumé

The most represented components of clathrin-coated vesicles (CCVs) are clathrin triskelia and the adaptors clathrin assembly lymphoid myeloid leukemia protein (CALM) and the heterotetrameric complex AP2. Investigation of the dynamics of AP180-amino-terminal-homology (ANTH) recruitment during CCV formation has been hampered by CALM toxicity upon overexpression. We used knock-in gene editing to express a C-terminal-attached fluorescent version of CALM, while preserving its endogenous expression levels, and cutting-edge live-cell microscopy approaches to study CALM recruitment at forming CCVs. Our results demonstrate that CALM promotes vesicle completion upon membrane tension increase as a function of the amount of this adaptor present. Since the expression of adaptors, including CALM, differs among cells, our data support a model in which the efficiency of clathrin-mediated endocytosis is tissue specific and explain why CALM is essential during embryogenesis and red blood cell development.

Identifiants

pubmed: 34155137
pii: 2010438118
doi: 10.1073/pnas.2010438118
pmc: PMC8237669
pii:
doi:

Substances chimiques

Adaptor Protein Complex 2 0
Monomeric Clathrin Assembly Proteins 0
PICALM protein, human 0
enhanced green fluorescent protein 0
Green Fluorescent Proteins 147336-22-9

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NCI NIH HHS
ID : P30 CA016058
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM127526
Pays : United States

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Nathan M Willy (NM)

Department of Physics, The Ohio State University, Columbus, OH 43210.

Federico Colombo (F)

College of Pharmacy, The Ohio State University, Columbus, OH 43210.

Scott Huber (S)

Department of Physics, The Ohio State University, Columbus, OH 43210.

Anna C Smith (AC)

College of Pharmacy, The Ohio State University, Columbus, OH 43210.

Erienne G Norton (EG)

College of Pharmacy, The Ohio State University, Columbus, OH 43210.

Comert Kural (C)

Department of Physics, The Ohio State University, Columbus, OH 43210; kural.1@osu.edu cocucci.1@osu.edu.
Interdisciplinary Biophysics Graduate Program, The Ohio State University, Columbus, OH 43210.

Emanuele Cocucci (E)

College of Pharmacy, The Ohio State University, Columbus, OH 43210; kural.1@osu.edu cocucci.1@osu.edu.
Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210.

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Classifications MeSH