Maintenance of the intestinal tube in Caenorhabditis elegans: the role of the intermediate filament protein IFC-2

Hüsken, Katrin; Wiesenfahrt, Tobias; Abraham, Christian; Windoffer, Reinhard; Bossinger, Olaf; Leube, Rudolf E.

doi:10.1111/j.1432-0436.2008.00264.x

Cited by 45 publications

(72 citation statements)

References 44 publications

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“…Most importantly, the C. elegans system is best suited to perform genetic screens for factors determining IF organization which should eventually succeed in the identification of regulatory pathways. The most simple inroad would be an optical screen using stable transgenic worms such as the previously described IFB-2::CFP expressing animals [Hüsken et al, 2008].…”

Section: Discussionmentioning

confidence: 99%

“…Much like the mammalian IF systems nematode IFs have diversified to fulfil cell type-specific tasks some of which are essential for organismal survival. Besides clarifying the underlying molecular pathways leading to lethality, the worm should also serve as a suitable system to study functions of the IF cytoskeleton that only become apparent in various types of stress situations or upon prolonged wear and tear as is the case in IFC-2-depleted animals [Hüsken et al, 2008]. And it is this buffering function that we consider to be the essential contribution of the abundant and diverse IF cytoskeleton to life of multicellular organisms.…”

Section: Discussionmentioning

confidence: 99%

“…Whether disruption of this link is the reason for compromised membrane targeting of apical membrane proteins in keratin knock-outs [Toivola et al, 2004[Toivola et al, , 2005 remains to be seen. Apparently, IFC-2 depletion in C. elegans is not sufficient to elicit such defects [Hüsken et al, 2008] and further, more radical depletion experiments are needed to assign such functions to the IF cytoskeleton in this organism.…”

Section: Intestinal Morphogenesis and The Cytoskeletonmentioning

confidence: 98%

“…In addition, the depicted worm synthesizes another fluorescent IF chimera which exhibits a very different distribution: the fluorescent proteins are present primarily in the subapical intestinal endotube where they are part of a dense filamentous network and accumulate to a lesser degree in the intestinal cytoplasm as granular structures [false pink color in Fig. 1 and movie 1; see also Hüsken et al, 2008].…”

Section: Diversity Of Intermediate Filaments In C Elegansmentioning

confidence: 99%

“…In contrast, all intestinal IFs are non-essential for larval development and their loss results only with very low penetrance in adult phenotypes in some instances [Karabinos et al, 2001 or develops over time [Hüsken et al, 2008] (Table I). A likely explanation for the comparatively mild defects is redundancy, since simultaneous down-regulation of several intestinal IFs gives rise to pronounced defects .…”

Section: Functional Consequences Of Intermediate Filament Protein Depmentioning

confidence: 99%

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Intermediate filaments in Caenorhabditis elegans

Carberry

Wiesenfahrt

Windoffer

et al. 2009

Cell Motil. Cytoskeleton

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Intermediate filaments (IFs) make up one of the three major fibrous cytoskeletal systems in metazoans. Numerous IF polypeptides are synthesized in cell typespecific combinations suggesting specialized functions. The review concentrates on IFs in the model organism Caenorhabditis elegans which carries great promise to elucidate the still unresolved mechanisms of IF assembly into complex networks and to determine IF function in a living organism. In contrast to Drosophila melanogaster, which lacks cytoplasmic IFs altogether, the nematode genome contains 11 genes coding for cytoplasmic IFs and only a single gene for a nuclear lamin. Its cytoplasmic IFs are expressed in developmentally and spatially defined patterns. As an example we present the case of the intestinal IFs which are abundant in the mechanically resilient endotube, a prominent feature of the C. elegans intestinal terminal web region. This IF-rich structure brings together all three cytoskeletal filaments that are integrated into a coherent entity by the C. elegans apical junction (CeAJ) thereby completely surrounding and stabilizing the intestinal lumen with its characteristic brush border. Concepts on the developmental establishment of the endotube in relation to polarization and its function for maintenance of epithelial integrity are discussed. Furthermore, possible connections of the cytoplasmic cytoskeleton to the nuclear lamin IFs and the importance of these links for nuclear positioning are summarized. Cell

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Intestinal Morphogenesis and The Cytoskeletonmentioning

confidence: 98%

Section: Diversity Of Intermediate Filaments In C Elegansmentioning

confidence: 99%

Section: Functional Consequences Of Intermediate Filament Protein Depmentioning

confidence: 99%

See 3 more Smart Citations

Intermediate filaments in Caenorhabditis elegans

Carberry

Wiesenfahrt

Windoffer

et al. 2009

Cell Motil. Cytoskeleton

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Assembly studies of six intestinal intermediate filament (IF) proteins B2, C1, C2, D1, D2, and E1 in the nematode C. elegans

Karabinos¹,

Schünemann

2017

Cytoskeleton

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The dimerisation properties of six intestine-expressed intermediate filament (IF) proteins (B2, C1, C2, D1, D2, E1) were analysed in blot overlay assay on membranes containing all of the eleven recombinant C. elegans IF proteins (A1, A2, A3, A4, B1, B2, C1, C2, D1, D2, and E1). The interactions detected in the blot assays exclusively comprise intestine-expressed IF proteins and the protein A4, which is found in the dauer larva intestine. About 86% of these interactions are heterotypic, while the remaining interactions relate to C1, C2, and D2 homodimers. These multiple modes of interaction were also supported by calculations of the numbers of possible interchain ionic interactions derived from the individual rod sequences. The results predict that the six B2, C1, C2, D1, D2, and E1 IF proteins are able to form as many as eleven different heteropolymeric and three homopolymeric IFs in the C. elegans intestine. This simple model of the intestinal IF meshwork enables us to speculate that our previously reported triple RNAi worms arrested or decreased their growth because of feeding reduction due to morphological defects of the mechanically compromised intestine.

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