Cited by 143Microtubule and mitosis dynamicsCellular Mechanics and InteractionsGenetic and Kidney Cyst Diseases

Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia

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Bowen, Jonathan R., Hwang, Daniel, Bai, Xiaobo, Roy, Dheeraj, Spiliotis, Elias T.·2011·Journal of Cell Biology

Abstract

Establishment of epithelial polarity requires the reorganization of the microtubule (MT) cytoskeleton from a radial array into a network positioned along the apicobasal axis of the cell. Little is known about the mechanisms that spatially guide the remodeling of MTs during epithelial polarization. Septins are filamentous guanine triphosphatases (GTPases) that associate with MTs, but the function of septins in MT organization and dynamics is poorly understood. In this paper, we show that in polarizing epithelia, septins guide the directionality of MT plus end movement by suppressing MT catastrophe. By enabling persistent MT growth, two spatially distinct populations of septins, perinuclear and peripheral filaments, steer the growth and capture of MT plus ends. This navigation mechanism is essential for the maintenance of perinuclear MT bundles and for the orientation of peripheral MTs as well as for the apicobasal positioning of MTs. Our results suggest that septins provide the directional guidance cues necessary for polarizing the epithelial MT network.

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  • The septin complex forms filaments associated with the microtubule cytoskeleton during interphase and diffuses within the cytoplasm upon cell rounding and microtubule de-polymerization.

    “The septin complex forms filaments associated with the microtubule cytoskeleton during interphase [51, 52] and diffuses within the cytoplasm upon cell rounding and microtubule de-polymerization (not shown).”
  • Septin becomes diffused within the cytoplasm upon suspension by trypsinization as microtubules depolymerize and becomes re-associated with them along with their re-formation upon cell spreading.

    “Septin becomes diffused within the cytoplasm upon suspension by trypsinization as microtubules depolymerize and becomes re-associated with them along with their re-formation upon cell spreading [51].”

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Authors
Bowen, J. R., Hwang, D., Bai, X., Roy, D., & Spiliotis, E. T.
Affiliations
Drexel University (US)
Corresponding author
Spiliotis, Elias T.
Venue
Journal of Cell Biology
Published
2011-07-25
Volume
194
Issue
2
Pages
187-197
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2099757502
Cited by
143
References
56
Citations by year
2026: 3 · 2025: 3 · 2024: 9 · 2023: 7 · 2022: 8 · 2021: 13 · 2020: 9 · 2019: 11 · 2018: 11 · 2017: 4 · 2016: 12 · 2015: 14 · 2014: 7 · 2013: 14 · 2012: 8
FWCI
5.98
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • National Institute of General Medical Sciences (R01GM097664)
  • National Institute of Neurological Disorders and Stroke (NS48090, R56NS048090, R01NS048090)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
Keywords
septins, microtubule organization, microtubule plus-end dynamics, microtubule catastrophe, epithelial polarity, microtubule growth
MeSH terms
Cells, Cultured, Epithelial Cells, Humans, Microtubules, Cell Polarity, Cell Cycle Proteins, Septins

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