Utations in emr-1 and lem-2 phenocopy all previously described lmn1 phenotypes (Liu et al., 2003; Margalit et al., 2005; Meyerzon et al., 2009b). We were therefore surprised that disrupting baf-1 or emr-1 and lem-2 did not bring about a nuclear migration phenotype. The inner nuclear membrane protein Ima1NET5Samp1 was previously shown to play a part in nuclear migration in mammalian tissue culture cells (Borrego-Pinto et al., 2012). It was also shown to interact having a SUN protein in both yeast and mammalian tissue culture (Hiraoka et al., 2011; Borrego-Pinto et al., 2012). Here we showed that the C. elegans homologue SAMP-1 plays a minor role in nuclear migration. Of interest, we discovered in spite of the requirement of lamin AC in tissue culture (Borrego-Pinto et al., 2012), C. elegans SAMP-1 localized independently of LMN-1. The SAMP-1 binding partners in the C. elegans nuclear envelope PubMed ID:http://www.ncbi.nlm.nih.gov/pubmed/21266802 remain to be determined (query marks in Figure 8). We suspect that baf-1, emr-1, lem-2, samp-1, along with other elements from the nucleoskeleton play partially redundant roles with lamin throughout nuclear migration. For that reason characterization of how the network of proteins forming the nucleoskeleton functions as a unit during nuclear migration needs LY3023414 price further investigation.Supplies AND Solutions C. elegans strains and RNA interferenceC. elegans had been cultured applying standard conditions, and N2 was employed as wild type (Brenner, 1974). Some nematode strains utilised in this function had been supplied by the Caenorhabditis Genetics Center (University of Minnesota, Minneapolis, MN), which can be funded by the National Institutes of Health National Center for Study Resources. The unc-84(n322), unc-84(e1174), unc-84(e1411), and unc-84(n369) alleles, from strains MT322, CB1174, CB1411, and MT369, respectively, had 
been previously described (Malone et al., 1999). The construct pSL589 was designed by cloning the XmaISphI fragment of the col-10 promoter from pOS12 (Spencer et al., 2001) into pPD96.04 to specifically drive expression of NLS::GFP::LacZ in embryonic hypodermal cells. This construct, pSL589, was injected into N2 worms after which integrated (Kage-Nakadai et al., 2012) to make strain UD469 (ycIs10[pcol-10nls::gfp::lacZ]). This outcrossed line was then crossed to unc-84(n322), unc-84(e1174), unc-84(e1411), and unc-84(n369) strains to create UD414, UD412, UD396, and UD399, respectively. UD87, expressing the full-length UNC-84 rescue construct, was employed because the beginning strain for SAMP-1 localization research in lmn-1(RNAi) (McGee et al., 2006; Chang et al., 2013. The lem-2(tm1582) deletion strain FX1582 and also the samp-1(tm2710) deletion strain FX2710 were kindly supplied by Shohei Mitani (National Bioresource Project at the Tokyo Women’s Medical University, Tokyo, Japan). samp-1(tm2710) was balanced with mIn1 [dpy-10(e128) mIs14] II from strain BS3493 to make strain UD470. The plbp-1 lmn-1::gfp strain UD324 was previously described (Fridolfsson and Starr, 2010). UD324 was crossed for the unc-84(n369) and unc-84(e1411) strains to create UD437 and UD436, respectively. For the lmn-1(RNAi) experiments, ycIs10 animals in an otherwise wild-type background were staged for 24 h post L4 at 20 and fed bacteria expressing dsRNA against lmn-1 in the Ahringer library (Fraser et al., 2000). Worms were transferred after 24 h, and also the plate from the initial 24 h was counted at 48 h. For emr-1(RNAi); lem-2(1582) treatment the very first 24 h was discardedMolecular Biology of the Cellmigration, whereas other individuals migrate p.