Peer-reviewed publications in the primary literature, exclusive of abstracts:
1. Holaska JM and Paschal BM. (1998) A cytosolic activity distinct from Crm1 mediates nuclear export of protein kinase inhibitor in permeabilized cells. Proc Natl Acad Sci USA 95, 14739-14744. http://www.pnas.org/content/95/25/14739.long
2. Black BE, Levesque L, Holaska JM, Wood TC, and Paschal BM. (1999) Identification of an NTF2-related factor that binds RanGTP and regulates nuclear protein export. Mol Cell Biol 19, 8616-8624. http://mcb.asm.org/content/19/12/8616.long
3. Lindsay ME, Holaska JM, Welch K, Paschal BM, and Macara IG. (2001) Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol 153, 1391-1402. http://jcb.rupress.org/content/153/7/1391.long
4. Black BE, Holaska JM, Rastinejad F, and Paschal BM. (2001) DNA binding domains in diverse nuclear receptors function as nuclear export signals. Curr Biol 11, 1749-1758. http://www.cell.com/current-biology/retrieve/pii/S0960982201005371
5. Black BE, Holaska JM, Levesque L, Ossareh-Nazari B, Dargemont C, and Paschal BM. (2001) NXT1 is necessary for the terminal step of Crm1-mediated nuclear export. J Cell Biol 152, 141-155. http://jcb.rupress.org/content/152/1/141.long
6. Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, and Paschal BM. (2001) Calreticulin is a receptor for nuclear export. J Cell Biol 152, 127-140. http://jcb.rupress.org/content/152/1/127.long
7. Brownawell AM, Holaska JM, Macara IG, and Paschal BM. (2002) The use of permeabilized cell systems to study nuclear transport. Meth Mol Biol 189, 209-229. http://www.springerlink.com/content/q41133j682500850/#section=82121&page=1
8. Holaska JM, Black BE, Rastinejad F, and Paschal BM. (2002) Ca2+-dependent nuclear export mediated by calreticulin. Mol Cell Biol 22, 6286-97. http://mcb.asm.org/content/22/17/6286.long
9. Mislow JM, Holaska JM, Kim MS, Lee KK, Segura-Totten M, Wilson KL, McNally EM. (2002) Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro. FEBS Lett 525, 135-40. http://www.sciencedirect.com/science/article/pii/S0014579302031058
10. Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, and Morris GE. (2003) Emerin interacts in vitro with the splicing-associated factor, YT521-B. Eur J Cell Biol 270, 2459-66. http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1033.2003.03617.x/full
11. Holaska JM, Lee KK, Kowalski AK, and Wilson KL. (2003) Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 278, 6969-75. http://www.jbc.org/content/278/9/6969.long
12. Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, and Hiraoka Y. (2004) Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Cell Biol 271, 1035-1045. http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.2004.04007.x/full
13. Holaska JM, Kowalski AK, and Wilson KL. (2004) Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear envelope. PloS Biol 2, 1354-1362. http://www.plosbiology.org/article/info%3Adoi%2F10.1371%2Fjournal.pbio.0020231
14. Holaska, JM and Wilson KL. (2006) Lmo7, an emerin-binding protein that shuttles between the cell surface and nucleus and regulates emerin transcription. Hum Mol Genet 15, 3459-3472. http://hmg.oxfordjournals.org/content/15/23/3459.long
15. Holaska, JM and Wilson KL. (2007) An emerin proteome: purification of distinct emerin-containing complexes from HeLa cells suggests a molecular basis for diverse roles including gene regulation, mRNA splicing, signaling and nuclear architecture. Biochemistry 46, 8897-8908. http://pubs.acs.org/doi/abs/10.1021/bi602636m
16. Puckelwartz MJ, Kessler E, Zhang Y, Hodzic D, Randles KN, Morris G, Earley JU, Hadhazy M, Holaska JM, Mewborn SK, Pytel P, McNally E. (2008) Disruption of nesprin-1 produces an Emery Dreifuss Muscular Dystrophy-like phenotype in mice. Hum Mol Genet 18, 607-620. http://hmg.oxfordjournals.org/content/18/4/607.long
17. Puckelwartz MJ, Kessler EJ, Kim G, DeWitt MM, Zhang Y, Earley JU, Depreux FF, Holaska JM, Mewborn SK, Pytel P, and McNally EM (2009). Nesprin-1 mutations in human and murine cardiomyopathy. J Mol Cell Cardiol 48, 600-608. http://www.sciencedirect.com/science/article/pii/S0022282809004817
18. Dedeic Z, Cetera M, Cohen TV, Holaska JM (2011). Emerin inhibits Lmo7 binding to the Pax3 and MyoD promoters and expression of myoblast differentiation genes. J Cell Sci 124, 1691-1702. http://jcs.biologists.org/content/124/10/1691.long
19. Demmerle J, Koch AJ, Holaska JM (2012). The nuclear envelope protein emerin binds to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. J Biol Chem, Epub ahead of print, May 8. http://www.jbc.org/content/early/2012/05/08/jbc.M111.325308.long
20. Koch AJ, Holaska JM (2012). Loss of emerin alters myogenic signaling and miRNA expression in mouse myogenic progenitors. PLoS One 7(5):e37262. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0037262
Peer-reviewed book chapters and review articles:
1. Holaska JM, Wilson KL, and Mansharamani M. (2002) The nuclear envelope, lamins, and nuclear assembly. Curr Opin Cell Biol 14, 357-64. http://www.sciencedirect.com/science/article/pii/S0955067402003290
2. Mansharamani M, Wilson KL, and Holaska JM. (2002) Dynamics of the Vertebrate Nuclear Envelope. In: Dynamics of Nuclear Envelope Assembly in Embryos and Somatic Cells. P. Collas, ed. (Landes Bioscience). http://www.springerlink.com/content/nu2l36126g218232/
3. Holaska, JM and Wilson KL. (2006) Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy. Anat Rec A Discov Mol Cell Evol Biol 288, 676-80. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2559942/?tool=pubmed
4. Holaska JM. (2008) Emerin and signaling via the nuclear lamina. Circ Res 103, 16-23. http://circres.ahajournals.org/content/103/1/16.long
Holaska Lab 