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Functional Characterization of Septin Complexes. / Akhmetova, K. A.; Chesnokov, I. N.; Fedorova, S. A.

In: Molekuliarnaia biologiia, Vol. 52, No. 2, 27.04.2018, p. 155-171.

Research output: Contribution to journal › Review article › peer-review

Harvard

Akhmetova, KA, Chesnokov, IN & Fedorova, SA 2018, 'Functional Characterization of Septin Complexes', Molekuliarnaia biologiia, vol. 52, no. 2, pp. 155-171. https://doi.org/10.7868/S0026898418020015

APA

Akhmetova, K. A., Chesnokov, I. N., & Fedorova, S. A. (2018). Functional Characterization of Septin Complexes. Molekuliarnaia biologiia, 52(2), 155-171. https://doi.org/10.7868/S0026898418020015

Vancouver

Akhmetova KA, Chesnokov IN, Fedorova SA. Functional Characterization of Septin Complexes. Molekuliarnaia biologiia. 2018 Apr 27;52(2):155-171. doi: 10.7868/S0026898418020015

Author

Akhmetova, K. A. ; Chesnokov, I. N. ; Fedorova, S. A. / Functional Characterization of Septin Complexes. In: Molekuliarnaia biologiia. 2018 ; Vol. 52, No. 2. pp. 155-171.

BibTeX

@article{51a177c91d064529b34b543f39f13093,
title = "Functional Characterization of Septin Complexes",
abstract = "Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments and associate with cell membranes, thus comprising newly acknowledged cytoskeletal system. Septins participate in a variety of cell processes and contribute to various pathophysiological states, including tumorigenesis and neurodegeneration. Here, we review the structural and functional properties of septins and the regulation of their dynamics with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytoskeletons. We also discuss how septins compartmentalize the cell by forming local protein-anchoring scaffolds and by providing barriers for the lateral diffusion of the membrane proteins.",
keywords = "septin complexes, septin filaments, septin scaffold, septins, Animals, Cell Membrane/enzymology, Humans, Multienzyme Complexes/genetics, Neoplasm Proteins/genetics, Neoplasms/enzymology, Neurodegenerative Diseases/enzymology, Septins/genetics",
author = "Akhmetova, {K. A.} and Chesnokov, {I. N.} and Fedorova, {S. A.}",
year = "2018",
month = apr,
day = "27",
doi = "10.7868/S0026898418020015",
language = "English",
volume = "52",
pages = "155--171",
journal = "Molekulyarnaya Biologiya",
issn = "0026-8984",
publisher = "Russian Academy of Sciences",
number = "2",

}

RIS

TY - JOUR

T1 - Functional Characterization of Septin Complexes

AU - Akhmetova, K. A.

AU - Chesnokov, I. N.

AU - Fedorova, S. A.

PY - 2018/4/27

Y1 - 2018/4/27

N2 - Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments and associate with cell membranes, thus comprising newly acknowledged cytoskeletal system. Septins participate in a variety of cell processes and contribute to various pathophysiological states, including tumorigenesis and neurodegeneration. Here, we review the structural and functional properties of septins and the regulation of their dynamics with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytoskeletons. We also discuss how septins compartmentalize the cell by forming local protein-anchoring scaffolds and by providing barriers for the lateral diffusion of the membrane proteins.

AB - Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments and associate with cell membranes, thus comprising newly acknowledged cytoskeletal system. Septins participate in a variety of cell processes and contribute to various pathophysiological states, including tumorigenesis and neurodegeneration. Here, we review the structural and functional properties of septins and the regulation of their dynamics with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytoskeletons. We also discuss how septins compartmentalize the cell by forming local protein-anchoring scaffolds and by providing barriers for the lateral diffusion of the membrane proteins.

KW - septin complexes

KW - septin filaments

KW - septin scaffold

KW - septins

KW - Animals

KW - Cell Membrane/enzymology

KW - Humans

KW - Multienzyme Complexes/genetics

KW - Neoplasm Proteins/genetics

KW - Neoplasms/enzymology

KW - Neurodegenerative Diseases/enzymology

KW - Septins/genetics

UR - http://www.scopus.com/inward/record.url?scp=85055078132&partnerID=8YFLogxK

UR - https://www.elibrary.ru/item.asp?id=32619490

U2 - 10.7868/S0026898418020015

DO - 10.7868/S0026898418020015

M3 - Review article

C2 - 29695686

AN - SCOPUS:85055078132

VL - 52

SP - 155

EP - 171

JO - Molekulyarnaya Biologiya

JF - Molekulyarnaya Biologiya

SN - 0026-8984

IS - 2

ER -

ID: 17180618