prikaz prve stranice dokumenta An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure
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Scientific paper - Original scientific paper
An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure
Journal of Biological Chemistry, 292 (2017); 9583-9598. https://doi.org/10.1074/jbc.M116.767939
Bradshaw, Nichola J.; Yerabham, Antony S. K.; Marreiros, Rita; Zhang, Tao; Nagel-Steget, Luitgard; Korth, Carsten

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Bradshaw, N. J., Yerabham, A. S. K., Marreiros, R., Zhang, T., Nagel Steget, L. & Korth, C. (2017). An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure. Journal of Biological Chemistry, 292., 9583-9598. doi: 10.1074/jbc.M116.767939

Bradshaw, Nichola J., et al. "An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure." Journal of Biological Chemistry, vol. 292, 2017, pp. 9583-9598. https://doi.org/10.1074/jbc.M116.767939

Bradshaw, Nichola J., Antony S. K. Yerabham, Rita Marreiros, Tao Zhang, Luitgard Nagel Steget and Carsten Korth. "An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure." Journal of Biological Chemistry 292 (2017): 9583-9598. https://doi.org/10.1074/jbc.M116.767939

Bradshaw, N. J., et al. (2017) 'An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure', Journal of Biological Chemistry, 292, pp. 9583-9598. doi: 10.1074/jbc.M116.767939

Bradshaw NJ, Yerabham ASK, Marreiros R, Zhang T, Nagel Steget L, Korth C. An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure. Journal of Biological Chemistry [Internet]. 2017 June 09 [cited 2024 November 07];292:9583-9598. doi: 10.1074/jbc.M116.767939

N. J. Bradshaw, A. S. K. Yerabham, R. Marreiros, T. Zhang, L. Nagel Steget and C. Korth, "An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure", Journal of Biological Chemistry, vol. 292, pp. 9583-9598, June 2017. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:193:118488. [Accessed: 07 November 2024]

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Metadata
Title (english)An unpredicted aggregation-critical region of the actinpolymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure
AuthorNichola J. Bradshaw
AuthorAntony S. K. Yerabham
AuthorRita Marreiros
AuthorTao Zhang
AuthorLuitgard Nagel-Steget
AuthorCarsten Korth
Author's institutionUniversity of Rijeka
(Faculty of Biotechnology and Drug Development)
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Biology
Abstract (english)
Aggregation of specific proteins in the brains of patients with chronic mental illness as a result of disruptions in proteostasis is an emerging theme in the study of schizophrenia in particular. Proteins including DISC1 (disrupted in schizophrenia 1) and dysbindin-1B are found in insoluble forms within brain homogenates from such patients. We recently identified TRIOBP-1 (Trio-binding protein 1, also known as Tara) to be another such protein through an epitope discovery and proteomics approach by comparing post-mortem brain material from schizophrenia patients and control individuals. We hypothesized that this was likely to occur as a result of a specific subcellular process and that it, therefore, should be possible to identify a region of the TRIOBP-1 protein that is essential for its aggregation to occur. Here, we probe the domain organization of TRIOBP-1, finding it to possess two distinct coiled-coil domains: the central and C-terminal domains. The central domain inhibits the depolymerization of F-actin and is also responsible for oligomerization of TRIOBP-1. Along with an N-terminal pleckstrin homology domain, the central domain affects neurite outgrowth. In neuroblastoma cells it was found that the aggregation propensity of TRIOBP-1 arises from its central domain, with a short “linker” region narrowed to within amino acids 324–348, between its first two coiled coils, as essential for the formation of TRIOBP-1 aggregates. TRIOBP-1 aggregation, therefore, appears to occur through one or more specific cellular mechanisms, which therefore have the potential to be of physiological relevance for the biological process underlying the development of chronic mental illness.
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionAccepted version
Journal titleJournal of Biological Chemistry
Numberingvol. 292, pp. 9583-9598
p-ISSN0021-9258
e-ISSN1083-351X
DOIhttps://doi.org/10.1074/jbc.M116.767939
URN:NBNurn:nbn:hr:193:118488
Publication2017-06-09
Document URLhttp://www.jbc.org/content/292/23/9583
Type of resourceText
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2018-09-14 11:30:18