Journal Article PUBDB-2024-00965

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Mutation-induced alterations of intra-filament subunit organization in vimentin filaments revealed by SAXS

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2019
Royal Soc. of Chemistry London

Soft matter 15(9), 1999 - 2008 () [10.1039/C8SM02281J]
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Abstract: Vimentin intermediate filaments constitute a distinct filament system in mesenchymal cells that is instrumental for cellular mechanics and migration. In vitro, the rod-like monomers assemble in a multi-step, salt-dependent manner into micrometer long biopolymers. To disclose the underlying mechanisms further, we employed small angle X-ray scattering on two recombinant vimentin variants, whose assembly departs at strategic points from the normal assembly route: (i) vimentin with a tyrosine to leucine change at position 117; (ii) vimentin missing the non-α-helical carboxyl-terminal domain. Y117L vimentin assembles into unit-length filaments (ULFs) only, whereas ΔT vimentin assembles into filaments containing a higher number of tetramers per cross section than normal vimentin filaments. We show that the shape and inner structure of these mutant filaments is significantly altered. ULFs assembled from Y117L vimentin contain more, less tightly bundled vimentin tetramers, and ΔT vimentin filaments preserve the number density despite the higher number of tetramers per filament cross-section.

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Contributing Institute(s):
  1. DOOR-User (DOOR ; HAS-User)
Research Program(s):
  1. 899 - ohne Topic (POF4-899) (POF4-899)
Experiment(s):
  1. DORIS Beamline B1 (DORIS III)

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Medline ; Creative Commons Attribution-NonCommercial CC BY-NC 4.0 ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Essential Science Indicators ; IF < 5 ; JCR ; National-Konsortium ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2024-02-27, last modified 2025-06-25


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