TY - JOUR
T1 - Filaments assembly of ectopically expressed Caenorhabditis elegans lamin within Xenopus oocytes
AU - Grossman, Einat
AU - Dahan, Idit
AU - Stick, Reimer
AU - Goldberg, Martin W.
AU - Gruenbaum, Yosef
AU - Medalia, Ohad
PY - 2012/1
Y1 - 2012/1
N2 - Lamins are the major components of the nuclear lamina, a filamentous layer underlying the inner nuclear membrane and attached to the peripheral chromatin. Lamins are required for maintaining nuclear shape and are involved in most nuclear activities. Here, we studied the 3D organization of the nuclear lamina formed upon the expression of. Caenorhabditis elegans lamin (Ce-lamin) within the nucleus of a. Xenopus laevis oocyte. We show that Ce-lamin forms an intricate 3D meshwork of 5-6. nm lamin protofilaments. The diverse protofilament interactions and organization may shed light upon the unique mechano-elastic properties of the nuclear lamina scaffold supporting the nuclear envelope. The Q159K Hutchinson-Gilford Progeria Syndrome-linked mutation alters interactions between protofilaments within the lamina, leading to the formation of more bundled arrays of less isotropically-oriented protofilaments. Using this system, we show for the first time the organization of lamin proteins that were translated and assembled within the environment of a living cell.
AB - Lamins are the major components of the nuclear lamina, a filamentous layer underlying the inner nuclear membrane and attached to the peripheral chromatin. Lamins are required for maintaining nuclear shape and are involved in most nuclear activities. Here, we studied the 3D organization of the nuclear lamina formed upon the expression of. Caenorhabditis elegans lamin (Ce-lamin) within the nucleus of a. Xenopus laevis oocyte. We show that Ce-lamin forms an intricate 3D meshwork of 5-6. nm lamin protofilaments. The diverse protofilament interactions and organization may shed light upon the unique mechano-elastic properties of the nuclear lamina scaffold supporting the nuclear envelope. The Q159K Hutchinson-Gilford Progeria Syndrome-linked mutation alters interactions between protofilaments within the lamina, leading to the formation of more bundled arrays of less isotropically-oriented protofilaments. Using this system, we show for the first time the organization of lamin proteins that were translated and assembled within the environment of a living cell.
KW - Caenorhabditis elegans lamin
KW - Cryo-electron tomography
KW - Intermediate filaments
KW - Nuclear lamina
KW - Protofilaments
UR - http://www.scopus.com/inward/record.url?scp=84855855189&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2011.11.002
DO - 10.1016/j.jsb.2011.11.002
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C2 - 22085746
AN - SCOPUS:84855855189
SN - 1047-8477
VL - 177
SP - 113
EP - 118
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 1
ER -