Research output: Contribution to journal › Review article › peer-review
Protein co-aggregation related to amyloids : Methods of investigation, diversity, and classification. / Bondarev, Stanislav A.; Antonets, Kirill S.; Kajava, Andrey V.; Nizhnikov, Anton A.; Zhouravleva, Galina A.
In: International Journal of Molecular Sciences, Vol. 19, No. 8, 2292, 04.08.2018.Research output: Contribution to journal › Review article › peer-review
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TY - JOUR
T1 - Protein co-aggregation related to amyloids
T2 - Methods of investigation, diversity, and classification
AU - Bondarev, Stanislav A.
AU - Antonets, Kirill S.
AU - Kajava, Andrey V.
AU - Nizhnikov, Anton A.
AU - Zhouravleva, Galina A.
PY - 2018/8/4
Y1 - 2018/8/4
N2 - Amyloids are unbranched protein fibrils with a characteristic spatial structure. Although the amyloids were first described as protein deposits that are associated with the diseases, today it is becoming clear that these protein fibrils play multiple biological roles that are essential for different organisms, from archaea and bacteria to humans. The appearance of amyloid, first of all, causes changes in the intracellular quantity of the corresponding soluble protein(s), and at the same time the aggregate can include other proteins due to different molecular mechanisms. The co-aggregation may have different consequences even though usually this process leads to the depletion of a functional protein that may be associated with different diseases. The protein co-aggregation that is related to functional amyloids may mediate important biological processes and change of protein functions. In this review, we survey the known examples of the amyloid-related co-aggregation of proteins, discuss their pathogenic and functional roles, and analyze methods of their studies from bacteria and yeast to mammals. Such analysis allow for us to propose the following co-aggregation classes: (i) titration: deposition of soluble proteins on the amyloids formed by their functional partners, with such interactions mediated by a specific binding site; (ii) sequestration: interaction of amyloids with certain proteins lacking a specific binding site; (iii) axial co-aggregation of different proteins within the same amyloid fibril; and, (iv) lateral co-aggregation of amyloid fibrils, each formed by different proteins.
AB - Amyloids are unbranched protein fibrils with a characteristic spatial structure. Although the amyloids were first described as protein deposits that are associated with the diseases, today it is becoming clear that these protein fibrils play multiple biological roles that are essential for different organisms, from archaea and bacteria to humans. The appearance of amyloid, first of all, causes changes in the intracellular quantity of the corresponding soluble protein(s), and at the same time the aggregate can include other proteins due to different molecular mechanisms. The co-aggregation may have different consequences even though usually this process leads to the depletion of a functional protein that may be associated with different diseases. The protein co-aggregation that is related to functional amyloids may mediate important biological processes and change of protein functions. In this review, we survey the known examples of the amyloid-related co-aggregation of proteins, discuss their pathogenic and functional roles, and analyze methods of their studies from bacteria and yeast to mammals. Such analysis allow for us to propose the following co-aggregation classes: (i) titration: deposition of soluble proteins on the amyloids formed by their functional partners, with such interactions mediated by a specific binding site; (ii) sequestration: interaction of amyloids with certain proteins lacking a specific binding site; (iii) axial co-aggregation of different proteins within the same amyloid fibril; and, (iv) lateral co-aggregation of amyloid fibrils, each formed by different proteins.
KW - Amyloid
KW - Co-aggregation
KW - Cross-seeding
KW - Functional amyloids
KW - Neurodegenerative diseases
KW - Prion
KW - RHIM
KW - cross-seeding
KW - NECROPTOSIS
KW - CYTOSKELETON
KW - INCLUSIONS
KW - ALZHEIMERS-DISEASE
KW - TAU
KW - ALPHA-SYNUCLEIN
KW - functional amyloids
KW - DROSOPHILA
KW - neurodegenerative diseases
KW - amyloid
KW - co-aggregation
KW - prion
KW - NF-KAPPA-B
KW - AGGREGATION
KW - PARKINSONS-DISEASE
UR - http://www.scopus.com/inward/record.url?scp=85052135558&partnerID=8YFLogxK
UR - http://www.mendeley.com/research/protein-coaggregation-related-amyloids-methods-investigation-diversity-classification
U2 - 10.3390/ijms19082292
DO - 10.3390/ijms19082292
M3 - Review article
C2 - 30081572
AN - SCOPUS:85052135558
VL - 19
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1422-0067
IS - 8
M1 - 2292
ER -
ID: 35906971