Regulation of proteolysis of intrinsically disordered proteins: physiological consequences
Само за регистроване кориснике
2021
Поглавље у монографији (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Proteolysis represents a primary recycling system for amino acids. Moreover, by controlling the protein turnover, proteolysis plays an important role in key cellular processes such as control of cell cycle, programmed cell death (including senescence) and response to various stimuli. In eukaryotic cells, most proteins are degraded by autophagy and 26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is determined by its structural features. Folded globular proteins in their native state are rarely degraded, however when misfolded, denatured or when an unstructured region is attached, the degradation is promoted. Proteins natively containing intrinsically disordered regions (IDRs) or completely lacking the stable secondary and tertiary structures are defined as intrinsically disordered proteins (IDPs). Due to their high intramolecular flexibility and plasticity, IDPs are involved in DNA metabolism, t...ranscriptional activation, autophagy, and signalling cascades related to response to various stimuli. In sessile organisms such as plants, IDPs enable prompt acclimation to external factors, including light perception, adaptation to oxidative stress and water loss, and regulation of protective, antioxidative and secondary metabolism. Binding of specific ligands and partners to particular IDP triggers structural changes and affects the stability of IDP, its susceptibility to proteolysis and aggregation-propensity. Theabnormal aggregation of several IDPs and altered proteolysis pathways are closely connected with serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's diseases. In this chapter, we discuss the current understanding of proteolytic processes of specific, well-characterised IDPs under different physiological states, emphasizing the influence of the microenvironment and ligands/partners on their conformation.
Кључне речи:
abiotic stress / amyloid-related neurodegenerative disorders / late embryogenesis proteins (LEAPs) / non-globular proteins / polyphenol oxidaseИзвор:
A closer look at proteolysis, 2021, 111-156Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200053 (Универзитет у Београду, Институт за мултидисциплинарна истраживања) (RS-MESTD-inst-2020-200053)
- LEAPSyn-SCI - Late Embryogenesis Abundant Proteins: Structural Characterisation and Interaction With Α-Synuclein (RS-ScienceFundRS-Promis-6039663)
Институција/група
Institut za multidisciplinarna istraživanjaTY - CHAP AU - Vidović, Marija AU - Milić Komić, Sonja PY - 2021 UR - http://rimsi.imsi.bg.ac.rs/handle/123456789/2928 AB - Proteolysis represents a primary recycling system for amino acids. Moreover, by controlling the protein turnover, proteolysis plays an important role in key cellular processes such as control of cell cycle, programmed cell death (including senescence) and response to various stimuli. In eukaryotic cells, most proteins are degraded by autophagy and 26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is determined by its structural features. Folded globular proteins in their native state are rarely degraded, however when misfolded, denatured or when an unstructured region is attached, the degradation is promoted. Proteins natively containing intrinsically disordered regions (IDRs) or completely lacking the stable secondary and tertiary structures are defined as intrinsically disordered proteins (IDPs). Due to their high intramolecular flexibility and plasticity, IDPs are involved in DNA metabolism, transcriptional activation, autophagy, and signalling cascades related to response to various stimuli. In sessile organisms such as plants, IDPs enable prompt acclimation to external factors, including light perception, adaptation to oxidative stress and water loss, and regulation of protective, antioxidative and secondary metabolism. Binding of specific ligands and partners to particular IDP triggers structural changes and affects the stability of IDP, its susceptibility to proteolysis and aggregation-propensity. Theabnormal aggregation of several IDPs and altered proteolysis pathways are closely connected with serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's diseases. In this chapter, we discuss the current understanding of proteolytic processes of specific, well-characterised IDPs under different physiological states, emphasizing the influence of the microenvironment and ligands/partners on their conformation. T2 - A closer look at proteolysis T1 - Regulation of proteolysis of intrinsically disordered proteins: physiological consequences EP - 156 SP - 111 UR - https://hdl.handle.net/21.15107/rcub_rimsi_2928 ER -
@inbook{ author = "Vidović, Marija and Milić Komić, Sonja", year = "2021", abstract = "Proteolysis represents a primary recycling system for amino acids. Moreover, by controlling the protein turnover, proteolysis plays an important role in key cellular processes such as control of cell cycle, programmed cell death (including senescence) and response to various stimuli. In eukaryotic cells, most proteins are degraded by autophagy and 26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is determined by its structural features. Folded globular proteins in their native state are rarely degraded, however when misfolded, denatured or when an unstructured region is attached, the degradation is promoted. Proteins natively containing intrinsically disordered regions (IDRs) or completely lacking the stable secondary and tertiary structures are defined as intrinsically disordered proteins (IDPs). Due to their high intramolecular flexibility and plasticity, IDPs are involved in DNA metabolism, transcriptional activation, autophagy, and signalling cascades related to response to various stimuli. In sessile organisms such as plants, IDPs enable prompt acclimation to external factors, including light perception, adaptation to oxidative stress and water loss, and regulation of protective, antioxidative and secondary metabolism. Binding of specific ligands and partners to particular IDP triggers structural changes and affects the stability of IDP, its susceptibility to proteolysis and aggregation-propensity. Theabnormal aggregation of several IDPs and altered proteolysis pathways are closely connected with serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's diseases. In this chapter, we discuss the current understanding of proteolytic processes of specific, well-characterised IDPs under different physiological states, emphasizing the influence of the microenvironment and ligands/partners on their conformation.", journal = "A closer look at proteolysis", booktitle = "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences", pages = "156-111", url = "https://hdl.handle.net/21.15107/rcub_rimsi_2928" }
Vidović, M.,& Milić Komić, S.. (2021). Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis, 111-156. https://hdl.handle.net/21.15107/rcub_rimsi_2928
Vidović M, Milić Komić S. Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis. 2021;:111-156. https://hdl.handle.net/21.15107/rcub_rimsi_2928 .
Vidović, Marija, Milić Komić, Sonja, "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences" in A closer look at proteolysis (2021):111-156, https://hdl.handle.net/21.15107/rcub_rimsi_2928 .