@article {68012,
	title = {Nuclear lamin isoforms differentially contribute to LINC complex-dependent nucleocytoskeletal coupling and whole-cell mechanics.},
	journal = {Proceedings of the National Academy of Sciences of the U.S.A.},
	volume = {119},
	year = {2022},
	month = {2022 Apr 19},
	pages = {e2121816119},
	abstract = {<p>SignificanceInteractions between the cell nucleus and cytoskeleton regulate cell mechanics and are facilitated by the interplay between the nuclear lamina and linker of nucleoskeleton and cytoskeleton (LINC) complexes. To date, the specific contribution of the four lamin isoforms to nucleocytoskeletal connectivity and whole-cell mechanics remains unknown. We discover that A- and B-type lamins distinctively interact with LINC complexes that bind F-actin and vimentin filaments to differentially modulate cortical stiffness, cytoplasmic stiffness, and contractility of mouse embryonic fibroblasts (MEFs). We propose and experimentally verify an integrated lamin-LINC complex-cytoskeleton model that explains cellular mechanical phenotypes in lamin-deficient MEFs. Our findings uncover potential mechanisms for cellular defects in human laminopathies and many cancers associated with mutations or modifications in lamin isoforms.</p>
},
	keywords = {Animals, Cell Nucleus, Cytoskeleton, Fibroblasts, Lamin Type A, Lamin Type B, Mice, Nuclear Lamina, Nuclear Matrix, Protein Isoforms},
	issn = {1091-6490},
	doi = {10.1073/pnas.2121816119},
	author = {Vahabikashi, Amir and Sivagurunathan, Suganya and Nicdao, Fiona Ann Sadsad and Han, Yu Long and Park, Chan Young and Kittisopikul, Mark and Wong, Xianrong and Tran, Joseph R and Gundersen, Gregg G and Reddy, Karen L and Luxton, G W Gant and Guo, Ming and Fredberg, Jeffrey J and Zheng, Yixian and Adam, Stephen A and Goldman, Robert D}
}
@article {6337,
	title = {Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1.},
	journal = {The Journal of Cell Biology},
	volume = {189},
	year = {2010},
	month = {2010 Jun 28},
	pages = {1087-96},
	abstract = {<p>The tumor suppressor protein adenomatous polyposis coli (APC) regulates cell protrusion and cell migration, processes that require the coordinated regulation of actin and microtubule dynamics. APC localizes in vivo to microtubule plus ends and actin-rich cortical protrusions, and has well-documented direct effects on microtubule dynamics. However, its potential effects on actin dynamics have remained elusive. Here, we show that the C-terminal "basic" domain of APC (APC-B) potently nucleates the formation of actin filaments in vitro and stimulates actin assembly in cells. Nucleation is achieved by a mechanism involving APC-B dimerization and recruitment of multiple actin monomers. Further, APC-B nucleation activity is synergistic with its in vivo binding partner, the formin mDia1. Together, APC-B and mDia1 overcome a dual cellular barrier to actin assembly imposed by profilin and capping protein. These observations define a new function for APC and support an emerging view of collaboration between distinct actin assembly-promoting factors with complementary activities.</p>
},
	keywords = {Actin Capping Proteins, Actins, Adenomatous Polyposis Coli Protein, Animals, Carrier Proteins, Fetal Proteins, Mice, Microfilament Proteins, NIH 3T3 Cells, Nuclear Proteins, Profilins, Protein Multimerization, Protein Transport},
	issn = {1540-8140},
	doi = {10.1083/jcb.201001016},
	author = {Okada, Kyoko and Bartolini, Francesca and Deaconescu, Alexandra M and Moseley, James B and Dogic, Zvonimir and Grigorieff, Nikolaus and Gundersen, Gregg G and Goode, Bruce L}
}
