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The BAR‐domain family of proteins: a case of bending and binding?: The membrane bending and GTPase-binding functions of proteins from the BAR-domain family
Open accessAbstract
BAR-domains recently took centre stage in science through a report on the crystal structure of this domain in Drosophila Amphiphysin. Though only weakly conserved at the sequence level, the structure of the BAR domain shows striking similarity to the GTPase-binding domain of Arfaptin 2, an effector of Rho- and Arf- GTPases. On the basis of this sequence and structural similarity, these two proteins have been classified as belonging to the same family, the BAR-domain family, and they probably also have similar functional characteristics. Presented here are the results of a database search for the sequence of the BAR domain of Amphiphysin and Arfaptin 2. This search identified a variety of related proteins, most of which are involved in intracellular transport and especially in endocytosis. For example, the BAR-domain family includes Endophilins, GTPase-activating proteins of the Centaurinbeta family and Oligophrenins, the adaptor proteins APPL1 and APPL2 that were recently shown to interact with the small GTPase Rab5, as well as members of the Sorting nexin family. On the basis of the structures of Amphiphysin and Arfaptin 2 and the cellular role of Amphiphysins in the early steps of endocytosis, the functions of the BAR domain have been defined as a dimerization motif and as sensing and inducing membrane curvature. However, data on Arfaptin 2 and now also on the Adaptor proteins APPL1 and 2 suggest that another function of the BAR domain is to bind to small GTPases.
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“However, the BAR domain is also known as a binding platform for several protein-protein interactions (37,38), suggesting that BACE1 is a novel cargo protein of BIN1 that is sorted from early endosomes to late endosomes/lysosomes.”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [37]
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Cites
Takai, Y., Sasaki, T., & Matozaki, T. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.153 · Cited by 2,511
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., & McMahon, H. T. (2004) · Science · doi:10.1126/science.1092586 · Cited by 1,636
Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. Thornton
Kelley, L. A., MacCallum, R. M., & Sternberg, M. J. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3741 · Cited by 1,464
Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei, K., Slepnev, V. I., Haucke, V., & Camilli, P. V. D. (1999) · Nature Cell Biology · doi:10.1038/9004 · Cited by 657
Generation of high curvature membranes mediated by direct endophilin bilayer interactions
Farsad, K., Ringstad, N., Takei, K., Floyd, S., Rose, K., & Camilli, P. V. D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200107075 · Cited by 602
APPL Proteins Link Rab5 to Nuclear Signal Transduction via an Endosomal Compartment
Miączyńska, M., Christoforidis, S., Giner, A., Shevchenko, A., Uttenweiler‐Joseph, S., Habermann, B. H., Wilm, M. S., Parton, R. G., & Zerial, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00117-5 · Cited by 553
Self-citationIRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
Miki, H., Yamaguchi, H., Suetsugu, S., & Takenawa, T. (2000) · Nature · doi:10.1038/35047107 · Cited by 550
Definition of general topological equivalence in protein structures
Šali, A., & Blundell, T. L. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90134-8 · Cited by 503
The role of ARF and Rab GTPases in membrane transport
Chavrier, P., & Goud, B. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80067-2 · Cited by 496
Amphiphysin 2 (Bin1) and T-Tubule Biogenesis in Muscle
Lee, E., Marcucci, M., DANIELL, L. W., Pypaert, M., Weisz, O. A., Ochoa, G.-C., Farsad, K., Wenk, M. R., & Camilli, P. V. D. (2002) · Science · doi:10.1126/science.1071362 · Cited by 463
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Weigert, R. (2012) · InTech eBooks · doi:10.5772/1233 · Cited by 10
Development of a Membrane Curvature-Sensing Peptide Based on a Structure–Activity Correlation Study
Kawano, K., Ogushi, M., Masuda, T., & Futaki, S. (2019) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c19-00465 · Cited by 10
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Gauthier, N. C., Ricci, V., Landraud, L., & Boquet, P. (2006) · Trends in Microbiology · doi:10.1016/j.tim.2006.05.002 · Cited by 10
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Phillips, D. A., Zacharoff, L. A., Hampton, C. M., Chong, G. W., Malanoski, A. P., Metskas, L. A., Xu, S., Bird, L. J., Eddie, B. J., Miklos, A. E., et al. (2021) · eLife · doi:10.7554/elife.60049 · Cited by 10
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Gnyliukh, N., Johnson, A., Nagel, M.-K., Monzer, A., Babić, D., Hlavata, A., Alotaibi, S. S., Isono, E., Loose, M., & Friml, J. (2024) · Journal of Cell Science · doi:10.1242/jcs.261720 · Cited by 9
Mahata, P., Singhal, L., Prasad, R. K., Kumar, K., Bakshi, S., Raj, P., Choudhary, H., & Biswas, A. (2022) · Materials Today Proceedings · doi:10.1016/j.matpr.2022.03.012 · Cited by 9
Force-control at cellular membranes
Galic, M., Begemann, I., Viplav, A., & Matis, M. (2014) · BioArchitecture · doi:10.1080/19490992.2015.1005524 · Cited by 10
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Bradshaw, C. R., Surendranath, V., & Habermann, B. H. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-466 · Cited by 8
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Wang, D., Yin, Y., Wu, J., Wang, X., & Zhong, Z. (2014) · Journal of Nanomaterials · doi:10.1155/2014/464925 · Cited by 8
Morgan, J. M., McCourt, P. C., Rankin, L., Swain, E., Rice, L. M., & Nickels, J. T. (2009) · Eukaryotic Cell · doi:10.1128/ec.00037-09 · Cited by 8
Woraratanadharm, T., Kmosek, S., & Banuett, F. (2018) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2018.09.002 · Cited by 8
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Gkourtsa, A., van den Burg, J., Strijbis, K., Avula, T., Bijvoets, S., Timm, D. D., Hochstenbach, F., & Distel, B. (2014) · Eukaryotic Cell · doi:10.1128/ec.00282-14 · Cited by 8
Barfly: Sculpting membranes at the Drosophila neuromuscular junction
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Hayn-Leichsenring, G., Liebig, C., Miething, A., Schulz, A., Kumar, S., Schwalbe, M., Eiberger, B., & Baader, S. L. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.05.038 · Cited by 7
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Sim, P. F., Chek, M. F., Nguyen, N., Nishimura, T., Inaba, T., Hakoshima, T., & Suetsugu, S. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad065 · Cited by 3
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Mattila, P. K. (2007) · Työväentutkimus Vuosikirja · Cited by 1
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Metadata
- Authors
- Habermann, B.
- Affiliations
- Max Planck Institute of Molecular Cell Biology and Genetics (DE)
- Corresponding author
- Habermann, Bianca
- ORCID
- Habermann, Bianca
- Venue
- The EMBO Reports
- Published
- 2004-03-01
- Volume
- 5
- Issue
- 3
- Pages
- 250-255
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1299016
- OpenAlex
- W2151624014
- Cited by
- 281
- References
- 24
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 6 · 2023: 8 · 2022: 10 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 8 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 14 · 2013: 9 · 2012: 19
- FWCI
- 9.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- BAR domain, amphiphysin, protein family classification, GTPase-binding domain, membrane curvature, endocytosis, intracellular transport, Rab5, APPL1, APPL2, sorting nexins, endophilin
- MeSH terms
- Amino Acid Sequence, Animals, Cell Membrane, Drosophila, Endocytosis, Molecular Sequence Data, Nerve Tissue Proteins, Phylogeny, Protein Conformation, Sequence Alignment, Protein Structure, Tertiary, Dimerization, GTP-Binding Protein Regulators, Monomeric GTP-Binding Proteins, Adaptor Proteins, Signal Transducing
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