Cited by 560Cellular transport and secretionReceptor Mechanisms and SignalingCaveolin-1 and cellular processes

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Clathrin

Kirchhausen, Tomas·2000·Annual Review of Biochemistry

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Abstract

▪ Abstract Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure. High-resolution structures of parts of clathrin, determined by X-ray crystallography, and lower-resolution images of assembled coats, determined by electron cryomicroscopy, now provide the information necessary to integrate various lines of evidence and to design experiments that test specific mechanistic notions. This review summarizes and illustrates the recent structural results and outlines what is known about coated-vesicle assembly in the context of this information.

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Inositol Hexakisphosphate Binds to Clathrin Assembly Protein 3 (AP-3/AP180) and Inhibits Clathrin Cage Assembly in Vitro
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AP180 and AP-2 Interact Directly in a Complex That Cooperatively Assembles Clathrin
Hao, W., Luo, Z. L., Zheng, L., Prasad, K., & Lafer, E. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22785 · Cited by 122
Clathrin assembly protein AP180: primary structure, domain organization and identification of a clathrin binding site.
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Identification of a clathrin binding subunit in the HA2 adaptor protein complex
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Functional Organization of Clathrin in Coats
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Self-citation
A dileucine‐like sorting signal directs transport into an AP‐3‐dependent, clathrin‐independent pathway to the yeast vacuole
Vowels, J. J., & Payne, G. S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2482 · Cited by 115
Coated pits and coated vesicles — sorting it all out
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Self-citation
Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
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Location and distribution of the light chains in clathrin trimers.
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Self-citation
Clathrin Light Chains LCA and LCB Are Similar, Polymorphic, and Share Repeated Heptad Motifs
Kirchhausen, T. L., Scarmato, P., Harrison, S. C., Monroe, J. J., Chow, E. P., Mattaliano, R. J., Ramachandran, K. L., Smart, J. E., Ahn, A. H., & Brosius, J. (1987) · Science · doi:10.1126/science.3563513 · Cited by 109
Self-citation
The Drosophila clathrin heavy chain gene: clathrin function is essential in a multicellular organism.
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Dynamin Assembles into Spirals under Physiological Salt Conditions upon the Addition of GDP and γ-Phosphate Analogues
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Clathrin heavy chain, light chain interactions.
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Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells.
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Immunofluorescent localization of 100K coated vesicle proteins.
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Clathrin self‐assembly is regulated by three light‐chain residues controlling the formation of critical salt bridges
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Clathrin-coated pits contain an integral membrane protein that binds the AP-2 subunit with high affinity.
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Clathrin heavy chain: molecular cloning and complete primary structure.
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Self-citation
ATP- and Cytosol-dependent Release of Adaptor Proteins from Clathrin-coated Vesicles: A Dual Role for Hsc70
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Synaptojanin Is the Major Constitutively Active Phosphatidylinositol-3,4,5-trisphosphate 5-Phosphatase in Rodent Brain
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Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions.
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Cytosolic and Membrane-associated Proteins Involved in the Recruitment of AP-1 Adaptors onto the Trans-Golgi Network
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Cytosol- and clathrin-dependent stimulation of endocytosis in vitro by purified adaptors.
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Bacterially expressed F1‐20/AP‐3 assembles clathrin into cages with a narrow size distribution: Implications for the regulation of quantal size during neurotransmission
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Structural domains of clathrin heavy chains.
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Self-citation
ISOLATION OF COATED VESICLES, PLAIN SYNAPTIC VESICLES, AND FLOCCULENT MATERIAL FROM A CRUDE SYNAPTOSOME FRACTION OF GUINEA PIG WHOLE BRAIN
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Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
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Configuration of clathrin trimers: Evidence from electron microscopy
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Self-citation
Clathrin assembly protein AP-3
Murphy, J.-E., Pleasure, I. T., Puszkin, S., Prasad, K., & Keen, J. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64336-8 · Cited by 69
Auxilin-Induced Interaction of the Molecular Chaperone Hsc70 with Clathrin Baskets
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Novel functions of clathrin light chains: clathrin heavy chain trimerization is defective in light chain-deficient yeast
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[22] Receptor-mediated endocytosis in semiintact cells
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Isolation of a new clathrin heavy chain gene with muscle-specific expression from the region commonly deleted in velo-cardio-facial syndrome
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Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11
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Limited proteolytic digestion of coated vesicle assembly polypeptides abolishes reassembly activity
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Sequence of the clathrin heavy chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function.
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Sequestration of the G protein βγ subunit complex inhibits receptor-mediated endocytosis
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High-Affinity Binding Of The AP-1 Adaptor Complex to Trans-Golgi Network Membranes Devoid Of Mannose 6-Phosphate Receptors
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The synapse-specific phosphoprotein F1-20 is identical to the clathrin assembly protein AP-3
Zhou, S., Tannery, N. H., Yang, J., Puszkin, S., & Lafer, E. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31438-8 · Cited by 53
Sorting out adaptors
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Disruption of the Clathrin Heavy Chain-Like Gene (CLTCL) Associated with Features of DGS/VCFS: A Balanced (21;22)(p12;q11) Translocation
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The calcium-binding site of clathrin light chains.
Näthke, I. S., Hill, B. L., Parham, P., & Brodsky, F. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44797-1 · Cited by 46
An image correlation analysis of the distribution of clathrin associated adaptor protein (AP-2) at the plasma membrane
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Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers
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Self-citation
Coated-vesicle formation in vitro: Conflicting results using different assays
Schmid, S. L. (1993) · Trends in Cell Biology · doi:10.1016/0962-8924(93)90129-o · Cited by 42
The Interaction of Calmodulin with Clathrin-coated Vesicles, Triskelions, and Light Chains
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Cloning and Characterization of a Novel Human Clathrin Heavy Chain Gene (CLTCL)
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Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3.
Scarmato, P., & Kirchhausen, T. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39644-9 · Cited by 30
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Characterization of the Clathrin Heavy Chain from Dictyostelium discoideum
O’Halloran, T. J., & Anderson, R. G. W. (1992) · DNA and Cell Biology · doi:10.1089/dna.1992.11.321 · Cited by 28
Light-chain independent binding of adaptors, AP180 and auxilin to clathrin
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Boa constrictor or rattlesnake?
Kirchhausen, T. L. (1999) · Nature · doi:10.1038/18989 · Cited by 23
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Mosquito clathrin heavy chain: analysis of protein structure and developmental expression in the ovary during vitellogenesis
Kokoza, V. A., Snigirevskaya, E. S., & Raikhel, A. S. (1997) · Insect Molecular Biology · doi:10.1046/j.1365-2583.1997.00191.x · Cited by 18
A Modulatory Role for Clathrin Light Chain Phosphorylation in Golgi Membrane Protein Localization during Vegetative Growth and during the Mating Response ofSaccharomyces cerevisiae
Chu, D. S., Pishvaee, B., & Payne, G. S. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.3.713 · Cited by 14
Probing the Phosphoinositide Binding Site of the Clathrin Assembly Protein AP-2 with Photoaffinity Labels
Profit, A. A., Chen, J., Gu, Q.-M., Chaudhary, A., Prasad, K., Lafer, E. M., & Prestwich, G. D. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0796 · Cited by 11

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Authors: Kirchhausen, T.
Affiliations: Harvard University (US)
Corresponding author: Kirchhausen, Tomas
ORCID: Kirchhausen, Tomas
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2000-06
Volume: 69
Issue: 1
Pages: 699-727
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.69.1.699
OpenAlex: W4251652273
Cited by: 560
References: 148
Citations by year: 2026: 15 · 2025: 11 · 2024: 9 · 2023: 11 · 2022: 12 · 2021: 22 · 2020: 12 · 2019: 10 · 2018: 22 · 2017: 12 · 2016: 17 · 2015: 12 · 2014: 22 · 2013: 28 · 2012: 17
FWCI: 2.68
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords: clathrin, clathrin-coated vesicles, endocytic receptor, X-ray crystallography, cryo-electron microscopy, endocytosis
MeSH terms: Amino Acid Sequence, Animals, Clathrin, Coated Pits, Cell-Membrane, Humans, Models, Molecular, Sequence Homology, Amino Acid, Protein Structure, Quaternary

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