Wataru Nunomura

Summary

Affiliation: Akita University School of Medicine
Country: Japan

Publications

  1. doi Phosphatidylinositol-4,5 bisphosphate (PIP2) inhibits apo-calmodulin binding to protein 4.1
    Wataru Nunomura
    Center for Geo Environmental Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan Electronic address
    Biochem Biophys Res Commun 446:434-40. 2014
  2. doi Unique Structural Changes in Calcium-Bound Calmodulin Upon Interaction with Protein 4.1R FERM Domain: Novel Insights into the Calcium-dependent Regulation of 4.1R FERM Domain Binding to Membrane Proteins by Calmodulin
    Wataru Nunomura
    Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Tegata Gakuên 1 1, Akita, 010 8502, Japan
    Cell Biochem Biophys 69:7-19. 2014
  3. doi Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes
    Wataru Nunomura
    Center for Geo Environmental Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan
    Cell Biochem Biophys 66:545-58. 2013
  4. doi Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na(+)/H(+) exchanger isoform 1)
    Wataru Nunomura
    Department of Cell and Tissue Biology, University of California San Francisco, San Francisco, CA, USA
    Biochem J 446:427-35. 2012
  5. doi Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: novel insights into the biological significance of the calcium-independent binding of calmodulin to protein 4.1R
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, Kawada 8 1, Shinjuku, Tokyo 162 8666, Japan
    Biochem J 440:367-74. 2011
  6. ncbi Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): unique binding properties with transmembrane proteins and calmodulin
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, Kawada 8 1, Shinjuku, Tokyo 162 8666, Japan
    Comp Biochem Physiol B Biochem Mol Biol 148:124-38. 2007
  7. doi Two different unique cardiac isoforms of protein 4.1R in zebrafish, Danio rerio, and insights into their cardiac functions as related to their unique structures
    Kenji Murata
    Department of Animal Science, University of California, Davis, CA, USA
    Dev Growth Differ 52:591-602. 2010
  8. doi Marked difference in membrane-protein-binding properties of the two isoforms of protein 4.1R expressed at early and late stages of erythroid differentiation
    Wataru Nunomura
    Department of Biochemistry, School of Medicine, Tokyo Women s Medical University, Tokyo 162 8666, Japan
    Biochem J 417:141-8. 2009
  9. doi Similarities and differences in the structure and function of 4.1G and 4.1R135, two protein 4.1 paralogues expressed in erythroid cells
    Wataru Nunomura
    Department of Biochemistry, School of Medicine, Tokyo Women s Medical University, Tokyo 162 8666, Japan
    Biochem J 432:407-16. 2010
  10. ncbi Regulation of protein 4.1R interactions with membrane proteins by Ca2+ and calmodulin
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, 8 1 Kawada, Shinjuku, Tokyo 162 8666, Japan
    Front Biosci 11:1522-39. 2006

Collaborators

Detail Information

Publications13

  1. doi Phosphatidylinositol-4,5 bisphosphate (PIP2) inhibits apo-calmodulin binding to protein 4.1
    Wataru Nunomura
    Center for Geo Environmental Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan Electronic address
    Biochem Biophys Res Commun 446:434-40. 2014
    ..We conclude that PIP2 may play an important role as a modulator of apo-CaM binding to 4.1R(80) throughout evolution. ..
  2. doi Unique Structural Changes in Calcium-Bound Calmodulin Upon Interaction with Protein 4.1R FERM Domain: Novel Insights into the Calcium-dependent Regulation of 4.1R FERM Domain Binding to Membrane Proteins by Calmodulin
    Wataru Nunomura
    Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Tegata Gakuên 1 1, Akita, 010 8502, Japan
    Cell Biochem Biophys 69:7-19. 2014
    ..We propose that these unique properties may account in part for the previously described Ca(2+)/CaM-dependent regulation of R30 binding to membrane proteins. ..
  3. doi Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes
    Wataru Nunomura
    Center for Geo Environmental Science, Graduate School of Engineering and Resource Science, Akita University, Akita, Japan
    Cell Biochem Biophys 66:545-58. 2013
    ..Taken together, these results show that Ca(2+)/CaM binding to GHP, and more specifically to pepG, has profound effects on other functional domains of 4.1G. ..
  4. doi Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na(+)/H(+) exchanger isoform 1)
    Wataru Nunomura
    Department of Cell and Tissue Biology, University of California San Francisco, San Francisco, CA, USA
    Biochem J 446:427-35. 2012
    ..1R FERM domain. We propose that 4.1R regulates NHE1 activity through a direct protein-protein interaction that can be modulated by intracellular pH and Na(+) and Ca(2+) concentrations...
  5. doi Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: novel insights into the biological significance of the calcium-independent binding of calmodulin to protein 4.1R
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, Kawada 8 1, Shinjuku, Tokyo 162 8666, Japan
    Biochem J 440:367-74. 2011
    ..15 K) respectively. These data support the notion that apo-CaM stabilizes R30 through interaction with its β-strand-rich C-lobe and provide a novel function for CaM, i.e. structural stabilization of 4.1R80...
  6. ncbi Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): unique binding properties with transmembrane proteins and calmodulin
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, Kawada 8 1, Shinjuku, Tokyo 162 8666, Japan
    Comp Biochem Physiol B Biochem Mol Biol 148:124-38. 2007
    ..Finally, we confirmed ZFR30 binding to erythrocyte plasma membrane proteins by pulling down ZFR30 with human erythrocyte inside-out vesicles (IOV). This study defines unique structural and functional properties for ZF4.1R...
  7. doi Two different unique cardiac isoforms of protein 4.1R in zebrafish, Danio rerio, and insights into their cardiac functions as related to their unique structures
    Kenji Murata
    Department of Animal Science, University of California, Davis, CA, USA
    Dev Growth Differ 52:591-602. 2010
    ..These results indicate that the gene product of ZF4.1RH3 is essential for normal morphological shape of the developing heart and to support the repetitive cycles of its muscle contraction and relaxation...
  8. doi Marked difference in membrane-protein-binding properties of the two isoforms of protein 4.1R expressed at early and late stages of erythroid differentiation
    Wataru Nunomura
    Department of Biochemistry, School of Medicine, Tokyo Women s Medical University, Tokyo 162 8666, Japan
    Biochem J 417:141-8. 2009
    ..These findings enable us to offer potential new insights into the differential contribution of 4.1R isoforms to membrane assembly during terminal erythroid differentiation...
  9. doi Similarities and differences in the structure and function of 4.1G and 4.1R135, two protein 4.1 paralogues expressed in erythroid cells
    Wataru Nunomura
    Department of Biochemistry, School of Medicine, Tokyo Women s Medical University, Tokyo 162 8666, Japan
    Biochem J 432:407-16. 2010
    ..We suggest that expression of the two paralogues of protein 4.1 with different affinities for band 3 and glycophorin C is likely to play a role in assembly of these two membrane proteins during terminal erythroid differentiation...
  10. ncbi Regulation of protein 4.1R interactions with membrane proteins by Ca2+ and calmodulin
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, 8 1 Kawada, Shinjuku, Tokyo 162 8666, Japan
    Front Biosci 11:1522-39. 2006
    ..1R. Finally, we give insights into the potential roles of 4.1R in the dynamic organization of the membrane skeleton viewed as a complex system...
  11. pmc Enucleation of human erythroblasts involves non-muscle myosin IIB
    Kumi Ubukawa
    Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan
    Blood 119:1036-44. 2012
    ..These data indicate that NMHC IIB among the isoforms is involved in the enucleation of human erythroblasts...
  12. doi Zinc-L-carnosine binds to molecular chaperone HSP70 and inhibits the chaperone activity of the protein
    Asami Haga
    Department of Life Science, Graduate School and Faculty of Engineering and Resource Science, Akita University, Akita 010 8502, Japan
    J Biochem 154:249-56. 2013
    ..It has been suggested that Polaprezinc binds to HSP70 especially in the N-domains, suppresses the chaperone activity and delays an ATPase activities of HSP70...
  13. pmc Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis
    Wataru Nunomura
    Department of Biochemistry, Tokyo Women s Medical University, Kawada 8 1, Shinjuku, Tokyo 162 8666, Japan
    Int J Cell Biol 2011:943272. 2011
    ..Interestingly, the HP region is an unstructured domain. Here we present an overview of the differences and similarities between 4.1 isoforms and paralogs. We also discuss the biological significance of unstructured domains...