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Clathrin
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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“The AP1 complex functions in the intracellular transport of cargo proteins between the trans-Golgi apparatus and endosomes by linking clathrin to the cargo proteins during vesicle membrane formation (Kirchhausen, 2000), and is important for the somatodendritic transport of proteins required for neuronal polarity (Farias et al., 2012).”
From A Highly Conserved Program of Neuronal Microexons Is Misregulated in Autistic Brains (2014) · cites this paper as Kirchhausen, 2000
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Cites
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor
Goodman, O. B., Krupnick, J. G., Santini, F., Gurevich, V. V., Penn, R. B., Gagnon, A. W., Keen, J. H., & Benovic, J. (1996) · Nature · doi:10.1038/383447a0 · Cited by 1,383
YOLK PROTEIN UPTAKE IN THE OOCYTE OF THE MOSQUITO AEDES AEGYPTI. L
Roth, T. F., & Porter, K. R. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.20.2.313 · Cited by 1,320
The structure of the G protein heterotrimer Giα1β1γ2
Wall, M. A., Coleman, D. E., Lee, E. N., Iñiguez-Lluhı́, J. A., Posner, B. A., Gilman, A. G., & Sprang, S. R. (1995) · Cell · doi:10.1016/0092-8674(95)90220-1 · Cited by 1,140
The 2.0 Å crystal structure of a heterotrimeric G protein
Lambright, D. G., Sondek, J., Bohm, A., Skiba, N. P., Hamm, H. E., & Sigler, P. B. (1996) · Nature · doi:10.1038/379311a0 · Cited by 1,136
Role of β-Arrestin in Mediating Agonist-Promoted G Protein-Coupled Receptor Internalization
Ferguson, S. S. G., Downey, W. E., Colapietro, A.-M., Barak, L. S., Ménard, L., & Caron, M. G. (1996) · Science · doi:10.1126/science.271.5247.363 · Cited by 974
Interaction of Tyrosine-Based Sorting Signals with Clathrin-Associated Proteins
Ohno, H., Stewart, J., Fournier, M.-C., Bosshart, H., Rhee, I. P., Miyatake, S., Saito, T., Gallusser, A., Kirchhausen, T. L., & Bonifacino, J. S. (1995) · Science · doi:10.1126/science.7569928 · Cited by 971
Self-citationDynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
Hinshaw, J. E., & Schmid, S. L. (1995) · Nature · doi:10.1038/374190a0 · Cited by 824
CLATHRIN-COATED VESICLE FORMATION AND PROTEIN SORTING: An Integrated Process
Schmid, S. L. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.511 · Cited by 800
Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
van der Bliek, A. M., & Meyerowrtz, E. M. (1991) · Nature · doi:10.1038/351411a0 · Cited by 776
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Orzech, E., Livshits, L., Leyt, J., Okhrimenko, H., Reich, V., Cohen, S., Weiss, A. M., Melamed‐Book, N., Lebendiker, M., Altschuler, Y., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101054200 · Cited by 15
Moulakakis, C., & Stamme, C. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90458.2008 · Cited by 15
Xu, Y., Liu, L., Ma, Y., Wang, C., Duan, F., Feng, J., Yin, H., Sun, L., Cao, Z., Jung, J., et al. (2024) · Aquatic Toxicology · doi:10.1016/j.aquatox.2024.107215 · Cited by 17
de Souza, L. B., daSilva, L. L. P., Jamur, M. C., & Oliver, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091868 · Cited by 14
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Sharma, V., Sharma, P., Selvapandiyan, A., & Salotra, P. (2015) · Molecular Microbiology · doi:10.1111/mmi.13253 · Cited by 14
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Sadasivan, S., Patil, A. J., Bromley, K. M., Hastie, P. G. R., Banting, G. S., & Mann, S. (2008) · Soft Matter · doi:10.1039/b803437k · Cited by 13
Lee, C.-L., Dang, J. W., Joo, K., & Wang, P. (2011) · Virus Research · doi:10.1016/j.virusres.2011.07.010 · Cited by 13
Döring, M., Loos, A., Schrader, N., Pfander, B., & Bauerfeind, R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04037.x · Cited by 14
Ohata, H., Ota, N., Shirouzu, M., Yokoyama, S., Yokota, J., Taya, Y., & Enari, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.029 · Cited by 13
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Exosomes: from biology to clinics
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Schu, P. V. (2001) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500055 · Cited by 12
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Bando, H., Shadrach, K. G., Rayborn, M. E., Crabb, J. W., & Hollyfield, J. G. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.09.008 · Cited by 11
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Metadata
- 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
- 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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