Research Topics
Species | Takashi DaihoSummaryAffiliation: Asahikawa Medical College Country: Japan Publications
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Detail Information
Publications
Critical role of Glu40-Ser48 loop linking actuator domain and first transmembrane helix of Ca2+-ATPase in Ca2+ deocclusion and release from ADP-insensitive phosphoenzymeTakashi Daiho
Department of Biochemistry, Asahikawa Medical College, Midorigaoka Higashi, Asahikawa, Japan
J Biol Chem 282:34429-47. 2007....- Deletions or specific substitutions of a few residues in the NH(2)-terminal region (Ala(3) to Thr(9)) of sarcoplasmic reticulum Ca(2+)-ATPase cause inactivation and rapid degradation of the enzyme expressed in COS-1 cellsT Daiho
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 274:23910-5. 1999.... - Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bondT Daiho
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 276:32771-8. 2001.... - Critical hydrophobic interactions between phosphorylation and actuator domains of Ca2+-ATPase for hydrolysis of phosphorylated intermediateGuoli Wang
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510, Japan
J Biol Chem 280:26508-16. 2005..The Tyr122-cluster, Ile235, and T181GE thus seem to have different roles and are critical in the successive events in processing phosphorylated intermediates to transport Ca2+... - Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase: changes in catalytic and transport sites during phStefania Danko
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 279:14991-8. 2004.... - Stable structural analog of Ca2+-ATPase ADP-insensitive phosphoenzyme with occluded Ca2+ formed by elongation of A-domain/M1'-linker and beryllium fluoride bindingTakashi Daiho
Department of Biochemistry, Asahikawa Medical University, Asahikawa 078 8510, Japan
J Biol Chem 285:24538-47. 2010..Results also demonstrate the critical structural roles of the Glu(40)-Ser(48) linker and of Mg(2+) at the catalytic site in these processes... - Val200 residue in Lys189-Lys205 outermost loop on the A domain of sarcoplasmic reticulum Ca2+-ATPase is critical for rapid processing of phosphoenzyme intermediate after loss of ADP sensitivitySanae Kato
Department of Biochemistry, Asahikawa Medical College, Asahikawa, 078-8510, Japan
J Biol Chem 278:9624-9. 2003..Results further suggest that these interactions, however, do not contribute much to domain organization in the dephosphorylated enzyme and thus would be mostly lost on E2P hydrolysis... - Deletions of any single residues in Glu40-Ser48 loop connecting a domain and the first transmembrane helix of sarcoplasmic reticulum Ca(2+)-ATPase result in almost complete inhibition of conformational transition and hydrolysis of phosphoenzyme intermediaTakashi Daiho
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510, Japan
J Biol Chem 278:39197-204. 2003..Results further suggest that the loop functions to coordinate this movement of A domain and the unique motion of M1 during the E1P to E2P transition... - Roles of interaction between actuator and nucleotide binding domains of sarco(endo)plasmic reticulum Ca(2+)-ATPase as revealed by single and swap mutational analyses of serine 186 and glutamate 439Xiaoyu Liu
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 284:25190-8. 2009.... - Comprehensive analysis of expression and function of 51 sarco(endo)plasmic reticulum Ca2+-ATPase mutants associated with Darier diseaseYuki Miyauchi
Departments of Biochemistry and Dermatology, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 281:22882-95. 2006..Our results also provided further insight into the structure-function relationship of SERCAs and revealed critical regions and residues of the enzyme... - Formation of the stable structural analog of ADP-sensitive phosphoenzyme of Ca2+-ATPase with occluded Ca2+ by beryllium fluoride: structural changes during phosphorylation and isomerizationStefania Danko
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 284:22722-35. 2009..Also, stable E1Ca(2).BeF(x) was produced from E2.BeF(3)(-) at 0.7 mm lumenal Ca(2+) by binding two Ca(2+) to lumenally oriented low affinity transport sites, as mimicking the reverse conversion E2P. Mg + 2Ca(2+) --> E1PCa(2).Mg... - Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+ -releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+ -ATPaseKazuo Yamasaki
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078 8510, Japan
J Biol Chem 283:29144-55. 2008..K(+) binding likely functions via producing the compactly organized structure, in this sense, similarly to Y122-HC... - Distinct types of abnormality in kinetic properties of three Darier disease-causing sarco(endo)plasmic reticulum Ca2+-ATPase mutants that exhibit normal expression and high Ca2+ transport activityKatsuhiko Sato
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510, Japan
J Biol Chem 279:35595-603. 2004..The results also provided further insight into the global nature of conformational changes of SERCAs for ATP-driven Ca(2+) transport... - [Mechanism of ca(2+) pump as revealed by mutations, development of stable analogs of phosphorylated intermediates, and their structural analyses]Hiroshi Suzuki
Department of Biochemistry, Asahikawa Medical College, Hokkaido, Japan
Yakugaku Zasshi 130:179-89. 2010..Genetic dysfunction of Ca(2+)-ATPase causes various isoform-specific diseases. In this manuscript, recent understanding of the Ca-ATPase will be reviewed... - Ca2+ release to lumen from ADP-sensitive phosphoenzyme E1PCa2 without bound K+ of sarcoplasmic reticulum Ca2+-ATPaseKazuo Yamasaki
Department of Biochemistry, Asahikawa Medical University, Asahikawa 078 8510, Japan
J Biol Chem 285:38674-83. 2010..These findings show that bound K(+) is critical for stabilizing both E1PCa(2) and E2P structures, thereby contributing to the structural changes that efficiently couple phosphoenzyme processing and Ca(2+) handling... - Multiple and distinct effects of mutations of Tyr122, Glu123, Arg324, and Arg334 involved in interactions between the top part of second and fourth transmembrane helices in sarcoplasmic reticulum Ca2+-ATPase: changes in cytoplasmic domain organization durKazuo Yamasaki
Department of Biochemistry, Asahikawa Medical College, Midorigaoka-Higashi, Asahikawa 078-8510, Japan
J Biol Chem 279:2202-10. 2004..During the Ca2+-transport cycle, the four residues seem to change interaction partners and thus contribute to the coordinated movements of the cytoplasmic and transmembrane domains... - ATP2C1 is specifically localized in the basal layer of normal epidermis and its depletion triggers keratinocyte differentiationMasaki Yoshida
Asahikawa Medical College, Department of Biochemistry, 2 1 1 1, Midorigaoka Higashi, Asahikawa, Hokkaido, 078 8510 Japan
J Dermatol Sci 43:21-33. 2006..ATP2C1 is a calcium/manganese-ATPase localized in the Golgi apparatus and known as responsible gene for Hailey-Hailey disease. But its localization and roles in the epidermis are not fully elucidated... - Remarkable stability of solubilized and delipidated sarcoplasmic reticulum Ca2+-ATPase with tightly bound fluoride and magnesium against detergent-induced denaturationKazuo Yamasaki
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510, Japan
J Biol Chem 277:13615-9. 2002..The present study thus reveals an essential property of the Mg(2+)/F(-)/Ca(2+)-ATPase complex, which will likely provide clues to understanding structure of the Ca(2+)-released form of phosphoenzyme intermediate at an atomic level... - Identification of arginyl residues located at the ATP binding site of sarcoplasmic reticulum Ca2+-ATPase. Modification with 1,2-cyclohexanedioneK Kimura
Department of Biochemistry, Asahikawa Medical College, Asahikawa 078, Japan
J Biol Chem 271:28933-41. 1996..This suggests that the arginyl residues involved in these inhibitions are distinct from that involved in the inhibition of the Ca2+-ATPase activity... - Organization of cytoplasmic domains of sarcoplasmic reticulum Ca(2+)-ATPase in E(1)P and E(1)ATP states: a limited proteolysis studyS Danko
Department of Biochemistry, Asahikawa Medical College, Midorigaokahigashi, Japan
FEBS Lett 505:129-35. 2001..Combined with previous results, we demonstrated that four states can be clearly distinguished by the susceptibility to three proteases, which will be very useful for establishing the conditions for structural studies...