Frances Brodsky: So you think you know all about clathrin?

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Abstract

Brodsky studies clathrin’s diverse biological functions.

Abstract

Brodsky studies clathrin’s diverse biological functions.

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A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism.

Alex M Plocik, Frances M. Brodsky, Raju Kucherlapati … (2009)

Intracellular trafficking of the glucose transporter GLUT4 from storage compartments to the plasma membrane is triggered in muscle and fat during the body's response to insulin. Clathrin is involved in intracellular trafficking, and in humans, the clathrin heavy-chain isoform CHC22 is highly expressed in skeletal muscle. We found a role for CHC22 in the formation of insulin-responsive GLUT4 compartments in human muscle and adipocytes. CHC22 also associated with expanded GLUT4 compartments in muscle from type 2 diabetic patients. Tissue-specific introduction of CHC22 in mice, which have only a pseudogene for this protein, caused aberrant localization of GLUT4 transport pathway components in their muscle, as well as features of diabetes. Thus, CHC22-dependent membrane trafficking constitutes a species-restricted pathway in human muscle and fat with potential implications for type 2 diabetes.

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Conformation switching of clathrin light chain regulates clathrin lattice assembly.

Jeremy Wilbur, Peter HWANG, Joel Ybe … (2010)

Clathrin-coated vesicle formation is responsible for membrane traffic to and from the endocytic pathway during receptor-mediated endocytosis and organelle biogenesis, influencing how cells relate to their environment. Generating these vesicles involves self-assembly of clathrin molecules into a latticed coat on membranes that recruits receptors and organizes protein machinery necessary for budding. Here we define a molecular mechanism regulating clathrin lattice formation by obtaining structural information from co-crystals of clathrin subunits. Low resolution X-ray diffraction data (7.9-9.0 A) was analyzed using a combination of molecular replacement with an energy-minimized model and noncrystallographic symmetry averaging. Resulting topological information revealed two conformations of the regulatory clathrin light chain bound to clathrin heavy chain. Based on protein domain positions, mutagenesis, and biochemical assays, we identify an electrostatic interaction between the clathrin subunits that allows the observed conformational variation in clathrin light chains to alter the conformation of the clathrin heavy chain and thereby regulates assembly. Copyright 2010 Elsevier Inc. All rights reserved.

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Folding and trimerization of clathrin subunits at the triskelion hub.

Amanda J. Stock, A Lupas, I Näthke … (1992)

The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four alpha helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.

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Journal

Journal ID (nlm-ta): J Cell Biol

Journal ID (iso-abbrev): J. Cell Biol

Journal ID (hwp): jcb

Title: The Journal of Cell Biology

Publisher: The Rockefeller University Press

ISSN (Print): 0021-9525

ISSN (Electronic): 1540-8140

Publication date (Print): 16 September 2013

Volume: 202

Issue: 6

Pages: 830-831

Author notes

csedwick@ 123456gmail.com

Text and Interview by Caitlin Sedwick

Article

Publisher ID: 2026pi

DOI: 10.1083/jcb.2026pi

PMC ID: 3776341

PubMed ID: 24043697

SO-VID: 4cf38055-425b-4591-84ff-39de41db19e6

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Frances Brodsky: So you think you know all about clathrin?

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Evolutionary Cell Biology

Most cited references 5

A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism.

Conformation switching of clathrin light chain regulates clathrin lattice assembly.

Folding and trimerization of clathrin subunits at the triskelion hub.

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