Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth.

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Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth. / Fuchino, Katsuya; Bagchi, Sonchita; Cantlay, Stuart; Sandblad, Linda; Wu, Di; Bergman, Jessica; Kamali-Moghaddam, Masood; Flärdh, Klas; Ausmees, Nora.

I: Proceedings of the National Academy of Sciences, Vol. 110, Nr. 21, 2013, s. E1889-E1897.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Fuchino, Katsuya ; Bagchi, Sonchita ; Cantlay, Stuart ; Sandblad, Linda ; Wu, Di ; Bergman, Jessica ; Kamali-Moghaddam, Masood ; Flärdh, Klas ; Ausmees, Nora. / Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth. I: Proceedings of the National Academy of Sciences. 2013 ; Vol. 110, Nr. 21. s. E1889-E1897.

RIS

TY - JOUR

T1 - Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth.

AU - Fuchino, Katsuya

AU - Bagchi, Sonchita

AU - Cantlay, Stuart

AU - Sandblad, Linda

AU - Wu, Di

AU - Bergman, Jessica

AU - Kamali-Moghaddam, Masood

AU - Flärdh, Klas

AU - Ausmees, Nora

PY - 2013

Y1 - 2013

N2 - Intermediate filament (IF)-like cytoskeleton emerges as a versatile tool for cellular organization in all kingdoms of life, underscoring the importance of mechanistically understanding its diverse manifestations. We showed previously that, in Streptomyces (a bacterium with a mycelial lifestyle similar to that of filamentous fungi, including extreme cell and growth polarity), the IF protein FilP confers rigidity to the hyphae by an unknown mechanism. Here, we provide a possible explanation for the IF-like function of FilP by demonstrating its ability to self-assemble into a cis-interconnected regular network in vitro and its localization into structures consistent with a cytoskeletal network in vivo. Furthermore, we reveal that a spatially restricted interaction between FilP and DivIVA, the main component of the Streptomyces polarisome complex, leads to formation of apical gradients of FilP in hyphae undergoing active tip extension. We propose that the coupling between the mechanism driving polar growth and the assembly of an IF cytoskeleton provides each new hypha with an additional stress-bearing structure at its tip, where the nascent cell wall is inevitably more flexible and compliant while it is being assembled and matured. Our data suggest that recruitment of cytoskeleton around a cell polarity landmark is a broadly conserved strategy in tip-growing cells.

AB - Intermediate filament (IF)-like cytoskeleton emerges as a versatile tool for cellular organization in all kingdoms of life, underscoring the importance of mechanistically understanding its diverse manifestations. We showed previously that, in Streptomyces (a bacterium with a mycelial lifestyle similar to that of filamentous fungi, including extreme cell and growth polarity), the IF protein FilP confers rigidity to the hyphae by an unknown mechanism. Here, we provide a possible explanation for the IF-like function of FilP by demonstrating its ability to self-assemble into a cis-interconnected regular network in vitro and its localization into structures consistent with a cytoskeletal network in vivo. Furthermore, we reveal that a spatially restricted interaction between FilP and DivIVA, the main component of the Streptomyces polarisome complex, leads to formation of apical gradients of FilP in hyphae undergoing active tip extension. We propose that the coupling between the mechanism driving polar growth and the assembly of an IF cytoskeleton provides each new hypha with an additional stress-bearing structure at its tip, where the nascent cell wall is inevitably more flexible and compliant while it is being assembled and matured. Our data suggest that recruitment of cytoskeleton around a cell polarity landmark is a broadly conserved strategy in tip-growing cells.

U2 - 10.1073/pnas.1305358110

DO - 10.1073/pnas.1305358110

M3 - Article

VL - 110

SP - E1889-E1897

JO - Proceedings of the National Academy of Sciences

T2 - Proceedings of the National Academy of Sciences

JF - Proceedings of the National Academy of Sciences

SN - 1091-6490

IS - 21

ER -