Research Topics
Genomes and Genes | Norihiro NakamuraSummaryAffiliation: Osaka University Country: Japan Publications
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Publications
Four Na+/H+ exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulationNorihiro Nakamura
Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560 0043, Japan
J Biol Chem 280:1561-72. 2005..We propose that the specific NHE isoforms contribute to the maintenance of the unique acidic pH values of the Golgi and post-Golgi compartments in the cell...
A novel kinesin-like protein, KIF1Bbeta3 is involved in the movement of lysosomes to the cell periphery in non-neuronal cellsMasafumi Matsushita
Department of Biological Sciences, Graduate School of Science, Osaka University, Machikaneyama cho 1 16, Toyonaka City, Osaka, Japan 560 0043
Traffic 5:140-51. 2004..These results indicate that KIF1Bbeta3 is involved in the translocation of lysosomes from perinuclear regions to the cell periphery...
The fourth transmembrane domain of the Helicobacter pylori Na+/H+ antiporter NhaA faces a water-filled channel required for ion transportNaoyuki Kuwabara
Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
J Biol Chem 279:40567-75. 2004..Furthermore, residues Ile-142 to Phe-144 may be important for the conformational change that accompanies ion transport in NhaA...
Characterization of the ion transport activity of the budding yeast Na+/H+ antiporter, Nha1p, using isolated secretory vesiclesRyuichi Ohgaki
Department of Biological Sciences, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560 0043, Japan
Biochim Biophys Acta 1712:185-96. 2005..The ion selectivity and the stoichiometry suggest a unique physiological role of Nha1p which is distinct from that of other known Na+/H+ antiporters...
A novel membrane protein capable of binding the Na+/H+ antiporter (Nha1p) enhances the salinity-resistant cell growth of Saccharomyces cerevisiaeKeiji Mitsui
Department of Biological Sciences, Graduate School of Science, Osaka University, Machikaneyama cho 1 16, Toynaka City, Osaka 560 0043, Japan
J Biol Chem 279:12438-47. 2004..These observations suggest that Cos3p is a novel membrane protein that can enhance salinity-resistant cell growth by interacting with the C1+C2 domain of Nha1p and thereby possibly activating the antiporter activity of this protein...
A conserved domain in the tail region of the Saccharomyces cerevisiae Na+/H+ antiporter (Nha1p) plays important roles in localization and salinity-resistant cell-growthKeiji Mitsui
Department of Biological Sciences, Graduate School of Science, Osaka University, 1 16 Machikaneyama cho, Toyonaka City, Osaka 560 0043
J Biochem 135:139-48. 2004..Based on the overall similarity of the two-domain structure of Nha1p to that of mammalian Na(+)/H(+) antiporters, the functional importance of domains proximal to the membrane region is discussed...
Two nuclear export signals specify the cytoplasmic localization of calcineurin B homologous protein 1Mana Nagita
Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560 0043
J Biochem 134:919-25. 2003..These results suggest that after CHP1 has entered the nucleus, it is exported to the cytoplasm in an NES-dependent manner...
A membrane-proximal region in the C-terminal tail of NHE7 is required for its distribution in the trans-Golgi network, distinct from NHE6 localization at endosomesNaomi Fukura
Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama cho 1 1, Toyonaka City, Osaka, 560 0043, Japan
J Membr Biol 234:149-58. 2010..These results suggest that two membrane proximal regions (residues 533-559 and 563-568) play an important role in targeting NHE7 to the TGN...
Detection of oligomerization and conformational changes in the Na+/H+ antiporter from Helicobacter pylori by fluorescence resonance energy transferAkira Karasawa
Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
J Biol Chem 280:41900-11. 2005..Dynamic interactions between HPNhaA monomers were detectable in membranes by FRET analysis, thus providing a new approach to study dynamic conformational changes in NhaA during antiport activity...
Oligomerization of the Saccharomyces cerevisiae Na+/H+ antiporter Nha1p: implications for its antiporter activityKeiji Mitsui
Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka City, Osaka 560 0043, Japan
Biochim Biophys Acta 1720:125-36. 2005..These results support the notion that Nha1p exists in membranes as a dimer and that the interaction of its monomers is important for its antiporter activity...
Nuclear localization of the serine/threonine kinase DRAK2 is involved in UV-induced apoptosisHiroshi Kuwahara
Department of Biological Sciences, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan
Biol Pharm Bull 29:225-33. 2006..Knockdown of DRAK2 expression by siRNA partially suppressed UV-induced apoptosis. These results suggest that DRAK2 plays a role in UV induced apoptosis...
The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-dependent manner by the calcium-binding protein CHPHiroshi Kuwahara
Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560 0043
J Biochem 134:245-50. 2003..These observations suggest that CHP negatively regulates the apoptosis-inducing protein kinase DRAK2 in a manner that depends on intracellular Ca(2+)-concentration...
Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensingYumi Tsuboi
Department of Biological Sciences, Graduate School of Science, Osaka University, Machikaneyama-cho 1-16, Toyonaka City, Osaka, Japan 560-0043
J Biol Chem 278:21467-73. 2003....
Calcineurin homologous protein isoform 2 (CHP2), Na+/H+ exchangers-binding protein, is expressed in intestinal epitheliumHiroki Inoue
Department of Biological Science, Graduate School of Science, Osaka University, Toyonaka, Osaka, Japan
Biol Pharm Bull 26:148-55. 2003..These results suggest that CHP2 functions in the absorptive epithelium for the intestine with NHE(s)...
Structurally and functionally conserved domains in the diverse hydrophilic carboxy-terminal halves of various yeast and fungal Na+/H+ antiporters (Nha1p)Shinya Kamauchi
Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan
J Biochem (Tokyo) 131:821-31. 2002..The results in this study suggest that the diverse hydrophilic region of yeast and fungal Nha1p has six conserved domains with conserved functions in terms of expression of Nha1p activity...
KIF1Bbeta2, capable of interacting with CHP, is localized to synaptic vesiclesNorihiro Nakamura
Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560 0043, Japan
J Biochem 132:483-91. 2002..These results suggest that KIF1Bbeta2, a novel CHP-interacting molecular motor, mediates the transport of synaptic vesicles in neuronal cells...
