Nuclear localization of magphinins, alternative splicing products of the human trophinin gene

Aoyama, Junya; Akazawa, Yusuke; Kasahara, Kousuke; Higashiyama, Yukihiro; Kikuchi, Ikue; Fukumoto, Yasunori; Saburi, Sakura; Nakayama, Yuji; Yamaguchi, Naoto

doi:10.1002/jcb.21446

Cited by 8 publications

(6 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Considering XAGE-1a, -1b and -1c share the common sequence and similar cellular localization, we thought that the NLS may be located on XAGE-1b, so, we analyzed the sequence of XAGE-1b for NLS by PSORT II program at http://psort.ims. u-tokyo.ac.jp (13,14). This analysis indicates that XAGE-1b has a classical type of NLS with 4 residue pattern (PKKK) or 7 residue pattern (PKKKNQQ) at 4th amino acid (Fig.…”

Section: Cellular Localization Of Four Xage Spliceosomes and Their Exmentioning

confidence: 80%

NLS-dependent and insufficient nuclear localization of XAGE-1 splice variants

Zhao

Tang²,

Liu³

et al. 2011

Oncol Rep

View full text Add to dashboard Cite

Abstract. XAGE-1 is a member of the cancer/testis antigen family and it was first identified by searching for the PAGE/ GAGE-related genes. Four transcript variants have been discovered and have a broad expression in cancer. As a prominent transcript, XAGE-1b is encoded by 81 amino acids with a molecular weight of 9 kDa. We determined the cellular localization of all four splice variants by confocal microscopy analysis. Among these, XAGE-1a, -1b and -1c showed distinct speckled nuclear localization, while XAGE-1d was distributed evenly both in the cytoplasm and nucleus. By deletion mutagenesis and site directed mutagenesis, we identified the bipartite nuclear localization signal and found that it contributes to the nuclear localization of XAGE-1 variants; but the nuclear localization signal (NLS) only cannot form the characterized distribution of XAGE-1b; amino acids 25-42 also play a role in the formation of nuclear speckles. XAGE-1b, the main transcript of XAGE-1, may act as a partner protein or a member of a protein complex, which plays a role in tumor development and progression.

show abstract

Section: Cellular Localization Of Four Xage Spliceosomes and Their Exmentioning

confidence: 80%

NLS-dependent and insufficient nuclear localization of XAGE-1 splice variants

Zhao

Tang²,

Liu³

et al. 2011

Oncol Rep

View full text Add to dashboard Cite

show abstract

“…The nomenclature for a full-length protein encoded by the trophinin gene has not been well-defined [11, 14], as experimental evidence for the expression of KIAA1114 in vitro or in vivo has never been provided by earlier studies. In the present study, we used the term “KIAA1114” to describe the full-length product translated from trophinin mRNA (Figure 1A).…”

Section: Resultsmentioning

confidence: 99%

“…Among the members of MAGE-D family, trophinin (also known as MAGE-D3 ) is particularly unique in that it can encode multiple translational products having pleiotropic functions in various biological processes. Previous reports have suggested that the presence of numerous translational initiation sites in trophinin mRNA and utilization of different alternative splicing could generate three major types of proteins – KIAA1114, TROPHININ, and MAGPHININs [10, 11]. Although a number of studies have been performed on dissecting the physiological role and function of TROPHININ in embryo implantation and cancer progression [12], only few studies have been conducted on a full-length protein encoded by the trophinin gene known as KIAA1114, whose cDNA coding sequence was initially identified from human brain [13].…”

Section: Introductionmentioning

confidence: 99%

KIAA1114, a full-length protein encoded by the trophinin gene, is a novel surface marker for isolating tumor-initiating cells of multiple hepatocellular carcinoma subtypes

et al. 2014

View full text Add to dashboard Cite

Identification of novel biomarkers for tumor-initiating cells (TICs) is of critical importance for developing diagnostic and therapeutic strategies against cancers. Here we identified the role of KIAA1114, a full-length translational product of the trophinin gene, as a distinctive marker for TICs in human liver cancer by developing a DNA vaccine-induced monoclonal antibody targeting the putative extracellular domain of KIAA1114. Compared with other established markers of liver TICs, KIAA1114 was unique in that its expression was detected in both alpha fetoprotein (AFP)-positive and AFP-negative hepatocellular carcinoma (HCC) cell lines with the expression levels of KIAA1114 being positively correlated to their tumorigenic potentials. Notably, KIAA1114 expression was strongly detected in primary hepatic tumor, but neither in the adjacent non-tumorous tissue from the same patient nor normal liver tissue. KIAA1114high cells isolated from HCC cell lines displayed TIC-like features with superior functional and phenotypic traits compared to their KIAA1114low counterparts, including tumorigenic abilities in xenotransplantation model, in vitro colony- and spheroid-forming capabilities, expression of stemness-associated genes, and migratory capacity. Our findings not only address the value of a novel antigen, KIAA1114, as a potential diagnostic factor of human liver cancer, but also as an independent biomarker for identifying TIC populations that could be broadly applied to the heterogeneous HCC subtypes.

show abstract

“…In both human and mouse, it gives rise to two distinct proteins, magphinin and trophinin [9,10]. Magphinin proteins are expressed in the male and female germ cells.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of mouse sperm motility by trophinin-binding peptide

Park

Yoon

Wang

et al. 2012

Reprod Biol Endocrinol

View full text Add to dashboard Cite

BackgroundTrophinin is an intrinsic membrane protein that forms a complex in the cytoplasm with bystin and tastin, linking it microtubule-associated motor dynein (ATPase) in some cell types. Previously, we found that human sperm tails contain trophinin, bystin and tastin proteins, and that trophinin-binding GWRQ (glycine, tryptophan, arginine, glutamine) peptide enhanced motility of human sperm.MethodsImmunohistochemistry was employed to determine trophinin protein in mouse spermatozoa from wild type mouse, by using spermatozoa from trophinin null mutant mice as a negative control. Multivalent 8-branched GWRQ (glycine, tryptophan, arginine, glutamine) peptide or GWRQ-MAPS, was chemically synthesized, purified by HPLC and its structure was confirmed by MALDI-TOF mass spectrometry. Effect of GWRQ-MAPS on mouse spermatozoa from wild type and trophinin null mutant was assessed by a computer-assisted semen analyzer (CASA).ResultsAnti-trophinin antibody stained the principal (central) piece of the tail of wild type mouse sperm, whereas the antibody showed no staining on trophinin null sperm. Phage particles displaying GWRQ bound to the principal piece of sperm tail from wild type but not trophinin null mice. GWRQ-MAPS enhanced motility of spermatozoa from wild type but not trophinin null mice. CASA showed that GWRQ-MAPS enhanced both progressive motility and rapid motility in wild type mouse sperm.ConclusionsPresent study established the expression of trophinin in the mouse sperm tail and trophinin-dependent effect of GWRQ-MAPS on sperm motility. GWRQ causes a significant increase in sperm motility.

show abstract

Nuclear localization of magphinins, alternative splicing products of the human trophinin gene

Cited by 8 publications

References 45 publications

NLS-dependent and insufficient nuclear localization of XAGE-1 splice variants

NLS-dependent and insufficient nuclear localization of XAGE-1 splice variants

KIAA1114, a full-length protein encoded by the trophinin gene, is a novel surface marker for isolating tumor-initiating cells of multiple hepatocellular carcinoma subtypes

Enhancement of mouse sperm motility by trophinin-binding peptide

Contact Info

Product

Resources

About