The DOI matches its Crossref record; 68 of the 70 references it cites were found in a registry or an index.
TBC proteins: GAPs for mammalian small GTPase Rab?
Abstract
The TBC (Tre-2/Bub2/Cdc16) domain was originally identified as a conserved domain among the tre-2 oncogene product and the yeast cell cycle regulators Bub2 and Cdc16, and it is now widely recognized as a conserved protein motif that consists of approx. 200 amino acids in all eukaryotes. Since the TBC domain of yeast Gyps [GAP (GTPase-activating protein) for Ypt proteins] has been shown to function as a GAP domain for small GTPase Ypt/Rab, TBC domain-containing proteins (TBC proteins) in other species are also expected to function as a certain Rab-GAP. More than 40 different TBC proteins are present in humans and mice, and recent accumulating evidence has indicated that certain mammalian TBC proteins actually function as a specific Rab-GAP. Some mammalian TBC proteins {e.g. TBC1D1 [TBC (Tre-2/Bub2/Cdc16) domain family, member 1] and TBC1D4/AS160 (Akt substrate of 160 kDa)} play an important role in homoeostasis in mammals, and defects in them are directly associated with mouse and human diseases (e.g. leanness in mice and insulin resistance in humans). The present study reviews the structure and function of mammalian TBC proteins, especially in relation to Rab small GTPases.
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“The apo structure (Fig. 5D) reveals an architecture highly conserved with other TBC domain proteins (Fischer et al., 2016; Fukuda, 2011; Park et al., 2011), with little conformational difference in comparison to the TSC1-complexed structures.”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Fukuda, 2011
In the citing paper
“Unlike other TBC proteins, which are generally known to act as GAPs for the Rab family of GTPases (Fukuda, 2011), TBC1D7 does not appear to have GAP activity relevant to the Rheb signaling axis upstream of mTORC1, instead likely increasing the sensitivity and responsivity of the entire complex to environmental signals.”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Fukuda, 2011
Citations
Cites
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
Rabs and their effectors: achieving specificity in membrane traffic
Grosshans, B. L., Ortiz, D., & Novick, P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601617103 · Cited by 1,005
Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation
Sano, H., Kane, S., Sano, E., Mı̂inea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., & Lienhard, G. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300063200 · Cited by 964
Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A–C
Hsu, C., Morohashi, Y., Yoshimura, S., Manrique‐Hoyos, N., Jung, S., Lauterbach, M. A., Bakhti, M., Grønborg, M., Möbius, W., Rhee, J., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911018 · Cited by 916
Evolution of the rab family of small GTP-binding proteins
Pereira‐Leal, J. B., & Seabra, M. C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5072 · Cited by 795
A Method to Identify Serine Kinase Substrates
Kane, S., Sano, H., Liu, S. C. H., Asara, J. M., Lane, W. S., Garner, C. C., & Lienhard, G. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200198200 · Cited by 529
Rab GTPases, intracellular traffic and disease
Seabra, M. C., Mules, E. H., & Hume, A. N. (2002) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02227-4 · Cited by 473
Mîinea, C. P., Sano, H., Kane, S., Sano, E., Fukuda, M., Peränen, J., Lane, W. S., & Lienhard, G. E. (2005) · Biochemical Journal · doi:10.1042/bj20050887 · Cited by 449
Self-citationBarr, F. A., & Lambright, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.007 · Cited by 434
Membrane traffic in the secretory pathway
Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 403
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Exercise, GLUT4, and skeletal muscle glucose uptake
Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407
Regulation of Small GTPases by GEFs, GAPs, and GDIs
Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245
Molecular mechanisms of ROS production and oxidative stress in diabetes
Newsholme, P., Cruzat, V. F., Keane, K. N., Carlessi, R., & de Bittencourt, P. I. H. (2016) · Biochemical Journal · doi:10.1042/bcj20160503c · Cited by 878
Rab family of small GTPases: an updated view on their regulation and functions
Homma, Y., Hiragi, S., & Fukuda, M. (2020) · FEBS Journal · doi:10.1111/febs.15453 · Cited by 482
Self-citationMultiple Roles of the Small GTPase Rab7
Guerra, F., & Bucci, C. (2016) · Cells · doi:10.3390/cells5030034 · Cited by 414
Metadata
- Authors
- Fukuda, M.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Fukuda, Mitsunori
- ORCID
- Fukuda, Mitsunori
- Venue
- Bioscience Reports
- Publisher
- Portland Press Ltd.
- Published
- 2011-01-14
- Volume
- 31
- Issue
- 3
- Pages
- 159-168
- ISSN
- 0144-8463 (ISSN-L)
- 1573-4935
- OpenAlex
- W2070101581
- Cited by
- 207
- References
- 70
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 16 · 2023: 7 · 2022: 12 · 2021: 16 · 2020: 22 · 2019: 11 · 2018: 12 · 2017: 17 · 2016: 19 · 2015: 9 · 2014: 14 · 2013: 13 · 2012: 18
- FWCI
- 1.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioscience Reports (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science
- 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- TBC domain, Rab GTPases, GTPase-activating protein, TBC1D1, small GTPases, Bub2, CDC16, insulin resistance, leanness, protein structure-function relationship
- MeSH terms
- Animals, Humans, Protein Structure, Tertiary, Monomeric GTP-Binding Proteins, rab GTP-Binding Proteins
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