Functional Characterization of Septin Complexes

K. A. Akhmetova, I. N. Chesnokov, S. A. Fedorova

Результат исследования: Научные публикации в периодических изданияхобзорная статьярецензирование

2 Цитирования (Scopus)


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.

Язык оригиналаанглийский
Страницы (с-по)137-150
Число страниц14
ЖурналMolecular Biology
Номер выпуска2
СостояниеОпубликовано - 1 мар 2018


Подробные сведения о темах исследования «Functional Characterization of Septin Complexes». Вместе они формируют уникальный семантический отпечаток (fingerprint).