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Plectin isoform 1-dependent nuclear docking of desmin networks affects myonuclear architecture and expression of mechanotransducers.

Staszewska I, Fischer I, Wiche G - Hum. Mol. Genet. (2015)

Bottom Line: We show that P1-mediated targeting of desmin IFs to myonuclei is essential for maintenance of their typically spheroidal architecture as well as their proper positioning and movement along the myofiber.Mechanistically, P1 is shown to specifically interact with the myonuclear membrane-associated (BAR domain-containing) protein endophilin B.Our results open a new perspective on cytoskeleton-nuclear crosstalk via specific cytolinker proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria.

No MeSH data available.


Related in: MedlinePlus

Partial colocalization of P1 and desmin at the outer nuclear membrane and disarray of perinuclear IF networks upon P1 deficiency. Wild-type and P1-deficient myofibers were subjected to double immunolabeling using antibodies to P1 and desmin; nuclei were visualized by staining with Hoechst dye. (A) Confocal and (B) deconvolved IFM images. Note partial colocalization of P1 and desmin at tail-like structures longitudinally extending from the nuclear equator of wild-type myofibers (arrowheads in A, upper row) and along Z-disk striations. Note disarray of desmin-positive structures in the vicinity of nuclei (arrowheads, lower row) as well as more spherical shapes of nuclei in P1-deficient compared with wild-type myofibers. Scale bars, 10 µm.
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DDV438F1: Partial colocalization of P1 and desmin at the outer nuclear membrane and disarray of perinuclear IF networks upon P1 deficiency. Wild-type and P1-deficient myofibers were subjected to double immunolabeling using antibodies to P1 and desmin; nuclei were visualized by staining with Hoechst dye. (A) Confocal and (B) deconvolved IFM images. Note partial colocalization of P1 and desmin at tail-like structures longitudinally extending from the nuclear equator of wild-type myofibers (arrowheads in A, upper row) and along Z-disk striations. Note disarray of desmin-positive structures in the vicinity of nuclei (arrowheads, lower row) as well as more spherical shapes of nuclei in P1-deficient compared with wild-type myofibers. Scale bars, 10 µm.

Mentions: To investigate the effects of P1 deficiency on perinuclear IF network organization, teased myofibers of wild-type and isoform P1-KO mice were subjected to co-immunostaining using isoform-specific anti-P1 and anti-desmin antibodies. In wild-type cells, P1 showed an accumulation at tail-like appendages associated with the equatorial regions of typically spheroidal and quite flat myonuclei, consistent with previous studies (15,19). Longitudinally extending toward the neighboring nuclei linearly arranged along the myofiber, these structures most probably represented the sarcoplasmic reticulum (Fig. 1A and B, upper rows; and Fig. 2A). The desmin-specific perinuclear staining pattern was very similar to that of P1, except that in this case the nuclear surface seemed to be continuously outlined, whereas this hardly applied for P1. These observations were consistent with the notion that both proteins were associated with the outer nuclear membrane/ER membrane system and that IFs formed cage-like structure around the nucleus.Figure 1.


Plectin isoform 1-dependent nuclear docking of desmin networks affects myonuclear architecture and expression of mechanotransducers.

Staszewska I, Fischer I, Wiche G - Hum. Mol. Genet. (2015)

Partial colocalization of P1 and desmin at the outer nuclear membrane and disarray of perinuclear IF networks upon P1 deficiency. Wild-type and P1-deficient myofibers were subjected to double immunolabeling using antibodies to P1 and desmin; nuclei were visualized by staining with Hoechst dye. (A) Confocal and (B) deconvolved IFM images. Note partial colocalization of P1 and desmin at tail-like structures longitudinally extending from the nuclear equator of wild-type myofibers (arrowheads in A, upper row) and along Z-disk striations. Note disarray of desmin-positive structures in the vicinity of nuclei (arrowheads, lower row) as well as more spherical shapes of nuclei in P1-deficient compared with wild-type myofibers. Scale bars, 10 µm.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4664173&req=5

DDV438F1: Partial colocalization of P1 and desmin at the outer nuclear membrane and disarray of perinuclear IF networks upon P1 deficiency. Wild-type and P1-deficient myofibers were subjected to double immunolabeling using antibodies to P1 and desmin; nuclei were visualized by staining with Hoechst dye. (A) Confocal and (B) deconvolved IFM images. Note partial colocalization of P1 and desmin at tail-like structures longitudinally extending from the nuclear equator of wild-type myofibers (arrowheads in A, upper row) and along Z-disk striations. Note disarray of desmin-positive structures in the vicinity of nuclei (arrowheads, lower row) as well as more spherical shapes of nuclei in P1-deficient compared with wild-type myofibers. Scale bars, 10 µm.
Mentions: To investigate the effects of P1 deficiency on perinuclear IF network organization, teased myofibers of wild-type and isoform P1-KO mice were subjected to co-immunostaining using isoform-specific anti-P1 and anti-desmin antibodies. In wild-type cells, P1 showed an accumulation at tail-like appendages associated with the equatorial regions of typically spheroidal and quite flat myonuclei, consistent with previous studies (15,19). Longitudinally extending toward the neighboring nuclei linearly arranged along the myofiber, these structures most probably represented the sarcoplasmic reticulum (Fig. 1A and B, upper rows; and Fig. 2A). The desmin-specific perinuclear staining pattern was very similar to that of P1, except that in this case the nuclear surface seemed to be continuously outlined, whereas this hardly applied for P1. These observations were consistent with the notion that both proteins were associated with the outer nuclear membrane/ER membrane system and that IFs formed cage-like structure around the nucleus.Figure 1.

Bottom Line: We show that P1-mediated targeting of desmin IFs to myonuclei is essential for maintenance of their typically spheroidal architecture as well as their proper positioning and movement along the myofiber.Mechanistically, P1 is shown to specifically interact with the myonuclear membrane-associated (BAR domain-containing) protein endophilin B.Our results open a new perspective on cytoskeleton-nuclear crosstalk via specific cytolinker proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria.

No MeSH data available.


Related in: MedlinePlus