Functional Characterization of Septin Complexes

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

In: Molecular Biology, Vol. 52, No. 2, 01.03.2018, p. 137-150.

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

Harvard

Akhmetova, KA, Chesnokov, IN & Fedorova, SA 2018, 'Functional Characterization of Septin Complexes', Molecular Biology, vol. 52, no. 2, pp. 137-150. https://doi.org/10.1134/S0026893317050028

APA

Akhmetova, K. A., Chesnokov, I. N., & Fedorova, S. A. (2018). Functional Characterization of Septin Complexes. Molecular Biology, 52(2), 137-150. https://doi.org/10.1134/S0026893317050028

Vancouver

Akhmetova KA, Chesnokov IN, Fedorova SA. Functional Characterization of Septin Complexes. Molecular Biology. 2018 Mar 1;52(2):137-150. doi: 10.1134/S0026893317050028

Author

Akhmetova, K. A. ; Chesnokov, I. N. ; Fedorova, S. A. / Functional Characterization of Septin Complexes. In: Molecular Biology. 2018 ; Vol. 52, No. 2. pp. 137-150.

BibTeX

@article{1996e05372c54dfabeea4a8f9b3cecea,

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",

author = "Akhmetova, {K. A.} and Chesnokov, {I. N.} and Fedorova, {S. A.}",

note = "Publisher Copyright: {\textcopyright} 2018, Pleiades Publishing, Inc.",

year = "2018",

month = mar,

day = "1",

doi = "10.1134/S0026893317050028",

language = "English",

volume = "52",

pages = "137--150",

journal = "Molecular Biology",

issn = "0026-8933",

publisher = "Maik Nauka-Interperiodica Publishing",

number = "2",

}

RIS

TY - JOUR

T1 - Functional Characterization of Septin Complexes

AU - Akhmetova, K. A.

AU - Chesnokov, I. N.

AU - Fedorova, S. A.

PY - 2018/3/1

Y1 - 2018/3/1

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

UR - http://www.scopus.com/inward/record.url?scp=85045526200&partnerID=8YFLogxK

U2 - 10.1134/S0026893317050028

DO - 10.1134/S0026893317050028

M3 - Review article

AN - SCOPUS:85045526200

VL - 52

SP - 137

EP - 150

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 12670449