Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins
| العنوان: | Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins |
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| المؤلفون: | Howard J. Worman, Edgar R. Gomes, Gregg G. Gundersen, Eric S. Folker, Jason C. Choi, Cecilia Östlund |
| المصدر: | Journal of Cell Science. 122:4099-4108 |
| بيانات النشر: | The Company of Biologists, 2009. |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | Microtubule-associated protein, Recombinant Fusion Proteins, LINC complex, Telomere-Binding Proteins, Emerin, Nerve Tissue Proteins, Biology, Mice, Fluorescence Resonance Energy Transfer, Animals, Protein Interaction Domains and Motifs, Cytoskeleton, Cells, Cultured, Mice, Knockout, Binding Sites, Nuclear Lamina, Membrane Proteins, Nuclear Proteins, Fluorescence recovery after photobleaching, Cell Biology, Surface Plasmon Resonance, Lamin Type A, Actins, Cell biology, Förster resonance energy transfer, Gene Knockdown Techniques, Multiprotein Complexes, Nuclear lamina, Microtubule-Associated Proteins, Lamin, Research Article, Fluorescence Recovery After Photobleaching |
| الوصف: | The linker of nucleoskeleton and cytoskeleton (LINC) complex is situated in the nuclear envelope and forms a connection between the lamina and cytoskeletal elements. Sun1, Sun2 and nesprin-2 are important components of the LINC complex. We expressed these proteins fused to green fluorescent protein in embryonic fibroblasts and studied their diffusional mobilities using fluorescence recovery after photobleaching. We show that they all are more mobile in embryonic fibroblasts from mice lacking A-type lamins than in cells from wild-type mice. Knockdown of Sun2 also increased the mobility of a short, chimeric form of nesprin-2 giant (mini-nesprin-2G), whereas the lack of emerin did not affect the mobility of Sun1, Sun2 or mini-nesprin-2G. Fluorescence resonance energy transfer experiments showed Sun1 to be more closely associated with lamin A than is Sun2. Sun1 and Sun2 had similar affinity for the nesprin-2 KASH domain in plasmon surface resonance (Biacore) experiments. This affinity was ten times higher than that previously reported between nesprin-2 and actin. Deletion of the actin-binding domain had no effect on mini-nesprin-2G mobility. Our data support a model in which A-type lamins and Sun2 anchor nesprin-2 in the outer nuclear membrane, whereas emerin, Sun1 and actin are dispensable for this anchoring. |
| تدمد: | 1477-9137 0021-9533 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6858a45384752b0deb3924932eb0bd8eTest https://doi.org/10.1242/jcs.057075Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....6858a45384752b0deb3924932eb0bd8e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14779137 00219533 |
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