679,751 research outputs found
Mammalian LIN-7 PDZ proteins associate with beta-catenin at the cell junctions of epithelia and neurons
The heterotrimeric PDZ complex containing LIN-2, LIN-7 and LIN-10 is known to be involved in the organization of epithelial and neuronal junctions in Caenorhabditis elegans and mammals. We report here that mammalian LIN-7 PDZ proteins form a complex with cadherin and β-catenin in epithelia and neurons. The association of LIN-7 with cadherin and β-catenin is Ca2+ dependent and is mediated by the direct binding of LIN-7 to the C-terminal PDZ target sequence of β-catenin, as demonstrated by means of co-immunoprecipitation experiments and in vitro binding assays with the recombinant glutathione S-transferase:LIN-7A. The presence of β-catenin at the junction is required in order to relocate LIN-7 from the cytosol to cadherin-mediated adhesions, thus indicating that LIN-7 junctional recruitment is β-catenin dependent and that one functional role of the binding is to localize LIN-7. Moreover, when LIN-7 is present at the β-catenin-containing junctions, it determines the accumulation of binding partners, thus suggesting the mechanism by which β-catenin mediates the organization of the junctional domai
Nan Lin and social capital
Nan Lin’s work on social capital is a significant, unique contribution. My purpose here is to explain that statement by looking at the work in historical context. Figure 2.1 is an index for much of the story to be told. The horizontal axis is time, beginning in 1975 when Nan Lin was at the State University of New York at Albany (now the University of Albany), through his 1990 move to Duke University, and on to 2010
A single E-box in the <i>Cel-lin-3</i> CRM is not sufficient for <i>lin-3</i> expression in the anchor cell of <i>C</i>. <i>elegans</i>.
(A) New cis-regulatory lin-3 alleles with deleted E-boxL and NHR or NHR and E-boxR. (B) Quantification of vulval induction in these new mutants. Note the complete absence of any induction in the recovered lin-3 alleles (n>30). Scorings of lin-3(1417) animals are the same as those reported in Fig 5 and are used here to indicate that this mutation leads to vulval hypo-induction rather than no induction at all. (C-D) smFISH in lin-3(mf72) (C) and N2 (D) animals. Green spots correspond to lin-3 transcripts and red spots to lag-2 that is used as an anchor cell marker. Blue is DAPI staining of nuclei. Note the absence of lin-3 expression in the anchor cell in the lin-3(mf72) mutant animal. Absence of lin-3 signal in the anchor cell was also confirmed for the other lin-3 alleles.</p
The stem cell E3-ligase Lin-41 promotes liver cancer progression through inhibition of microRNA-mediated gene silencing
Lin-41 is a stem cell-specific E3 ligase and a known target of the tumour suppressor microRNA (miRNA) let-7. Lin-41 was recently reported to mediate ubiquitylation and degradation of the miRNA pathway protein Ago2. We demonstrate that Lin-41 is over-expressed in hepatocellular carcinoma (HCC). Lin-41 over-expression correlates with high a-fetoprotein level, high tumour grade and high tumour stage and predicts early tumour recurrence. Lin-41 is a strong predictor of poor long-term survival for patients with HCC. Lin-41 knock-down by RNA interference in HCC cell lines Huh7 and Hep3B suppressed proliferation in vitro and reduced in vivo tumour growth in NOD/SCID mice. On the other hand, over-expression of Lin-41 in the HCC cell line SK-Hep1 enhanced tumourigenicity. Over-expression and knock-down of Lin-41 led to inverse changes in the levels of Ago1 and Ago2 proteins. Over-expression of Ago1 and Ago2 reduced in vivo tumour growth. Lin-41 over-expression suppressed let-7 activity in HCC cell lines and expression of Lin-41 enhanced the expression of let-7-regulated oncogenes c-Myc, Lin-28B, HMGA2 and type 1 insulin-like growth factor receptor (IGF1R). Expression of Lin-28B and c-Myc enhanced the expression of Lin-41. Chromatin immunoprecipitation and reporter assays revealed direct association of c-Myc with the Lin-41 promoter, resulting in transcriptional transactivation. Our results indicate that Lin-41 plays an important role in the growth of HCC by regulating RISC complex proteins Ago1 and Ago2 to inhibit miRNA-mediated gene silencing and promote the expression of oncogenic proteins. Lin-41 is also a strong prognostic factor for patients with HCC. Copyright (C) 2012 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd
Singaporemma bifurcata Lin & Li 2010
Singaporemma bifurcata Lin & Li, 2010 Figures 1A–H, 2A–E, 6F–f, 8A Singaporemma bifurcata Lin & Li, 2010: 26, figs 29–37 Examined material. Topotypes 11♂ 25♀ (NHMSU), CHINA: Guizhou, Suiyang, Wenquan Town, Guihua Village, Hejiao Cave, 28°15´N, 107°17´E, altitude 695 m, 17 April 2015, Y. Lin and H. Yang leg. Diagnosis. With the exception of S. wulongensis, male of S. bifurcata can be distinguished from all other congeners by the embolus with an asymmetrically furcate end (Fig. 6f vs. Fig. 6a–d, 6g –h), and female of S. bifurcata differs by the stubby, sclerotized central process (Fig. 8A vs. Figs. 5C–D, 7A–C, 9A–B). S. bifurcata similar to S. wulongensis in the shape of palpal bulb and the configuration of vulva, but male of S. bifurcata can be distinguished from that of S. wulongensis by the starting position of embolus (Fig. 6F vs. Fig. 6E, the position indicated by the blue arrow) and the unequal length of branches of embolic tip (Fig. 6f vs. Fig. 6e); female of S. bifurcata separated by the smaller, “Ω”-shaped inner vulval plate, and the shorter central process (Fig. 8A vs. Fig. 8B). Description. See Figs 1A–H, 2A–E, 6F–f, 8A and Lin & Li, 2010: 26. Distribution. China (Guizhou) (Fig. 10).Published as part of Yan, Fanhu & Lin, Yucheng, 2018, A review of the spider genus Singaporemma (Araneae: Tetrablemmidae), with the description of a new species, pp. 329-346 in Zootaxa 4392 (2) on page 334, DOI: 10.11646/zootaxa.4392.2.6, http://zenodo.org/record/119544
LIN-2/CASK binds to both ACR-16 and UNC-29 through SH3 domain.
(A) Summary of interactions by Yeast two-hybrid. Strong interaction (++); weak interaction (+), and no interactions (-) were indicated. (B) LIN-2A’s SH3 domain binds the ACR-16’s second intracellular loop (LoopII) in a Yeast two-hybrid assay. Y2HGold cells carrying indicated plasmids (Left) growing on selective media (-Trp/-Leu/-His/-Ade) is shown (Right). (C) LIN-2A’s SH3 domain binds the UNC-29’s second intracellular loop (LoopII) in the Yeast two-hybrid assay. (D-E) FRM-3 do not bind the ACR-16’s second intracellular loop (LoopII) (D) and UNC-29’s second intracellular loop (LoopII) (E) in the Yeast two-hybrid assay. (F-G) LIN-2A binds FRM-3 (F) and its FERM domain (G) requiring its PDZ domain, but not SH3 domain.</p
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