A5101723857- Cellular transport and secretion
- Endoplasmic Reticulum Stress and Disease
- Ubiquitin and proteasome pathways
- Protein Kinase Regulation and GTPase Signaling
- RNA regulation and disease
- Calpain Protease Function and Regulation
- S100 Proteins and Annexins
- Microtubule and mitosis dynamics
- Cellular Mechanics and Interactions
- PI3K/AKT/mTOR signaling in cancer
- Copper Interconnects and Reliability
- Ion channel regulation and function
- Semiconductor materials and devices
- Signaling Pathways in Disease
- Retinal Development and Disorders
- Fungal and yeast genetics research
- Peptidase Inhibition and Analysis
- Polyamine Metabolism and Applications
- Biotin and Related Studies
- RNA Research and Splicing
- Viral Infectious Diseases and Gene Expression in Insects
- 3D IC and TSV technologies
- Cell death mechanisms and regulation
- 14-3-3 protein interactions
- Pancreatic function and diabetes
Nagoya University
2015-2024
Toyota Kosei Hospital
2022-2024
Kumamoto University
2012
The University of Tokyo
2008
Toshiba (Japan)
1994-2006
Kobe University
1994-2004
Annexin A11 mutations, implicated in ALS, prevent binding to calcyclin and induce the formation of cytoplasmic inclusions.
A novel 450-kDa coiled-coil protein, CG-NAP (centrosome and Golgi localized PKN-associated protein), was identified as a protein that interacted with the regulatory region of kinase PKN, having catalytic domain homologous to C. contains two sets putative RII (regulatory subunit A)-binding motif. Indeed, tightly bound RIIα in HeLa cells. Furthermore, coimmunoprecipitated phosphatase 2A (PP2A), when one B PP2A (PR130) exogenously expressed COS7 also 1 Immunofluorescence analysis cells revealed...
Alix (ALG-2-interacting protein X) is a 95-kDa that interacts with an EF-hand type Ca2+-binding protein, ALG-2 (apoptosis-linked gene 2), through its C-terminal proline-rich region. In this study, we searched for proteins interact human AlixΔC (a truncated form not containing the region) by using yeast two-hybrid screen, and identified two similar proteins, CHMP4a CHMP4b (chromatin-modifying protein; charged multivesicular body protein), as novel binding partners of Alix. The interaction was...
PKN is a fatty acid- and Rho-activated serine/threonine protein kinase, having catalytic domain homologous to kinase C family. To identify components of the PKN-signaling pathway such as substrates regulatory proteins PKN, yeast two-hybrid strategy was employed. Using N-terminal region bait, cDNAs encoding actin cross-linking α-actinin, which lacked actin-binding domain, were isolated from human brain cDNA library. The responsible for interaction between α-actinin determined by in vitro...
CHMP6 (charged multivesicular body protein 6) is a human orthologue of yeast Vps (vacuolar sorting) 20, component ESCRT (endosomal sorting complex required for transport)-III. Various orthologues in organisms ranging from to humans contain the N-myristoylation consensus sequence at each N-terminus. Metabolic labelling HEK-293 (human embryonic kidney) cells showed incorporation [3H]myristate into fused C-terminally GFP (green fluorescent protein) (CHMP6–GFP). Interactions with another...
Mammalian phosphatidylcholine-specific phospholipase D1 (PLD1) is a signal transduction-activated enzyme thought to function in multiple cell biological settings including the regulation of membrane vesicular trafficking. PLD1 activated by small G proteins, ADP-ribosylation factor (ARF) and RhoA, protein kinase C-alpha (PKC-alpha). This stimulation has been proposed involve direct interaction take place at distinct site for each activator. In present study, we employed yeast two-hybrid...
PKN is a fatty acid-activated serine/threonine kinase that has catalytic domain highly homologous to of protein C in the carboxyl terminus and unique regulatory region amino terminus. Recently, we reported small GTP-binding Rho binds amino-terminal activates GTP-dependent manner, suggested located on downstream signal transduction pathway (Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Okawa, Iwamatsu, A., Kaibuchi, K.(1996) Science 271, 648-650; Watanabe, G., Saito,...
ALG-2 (apoptosis-linked gene 2) is a Ca2+-binding protein that belongs to the PEF (penta-EF-hand) family. Alix (ALG-2-interacting X)/AIP1 1), one of its binding partners, interacts with TSG101 and CHMP4 (charged multivesicular body 4), which are components ESCRT-I (endosomal sorting complex required for transport I) ESCRT-III respectively. In present study, we investigated association between ESCRT-I. By GST (glutathione S-transferase) pull-down assay using HEK-293T (human embryonic kidney...
All CHMPs (charged multivesicular body proteins) reported to date have common features: they all contain approx. 200 amino acid residues, coiled-coil regions and a biased distribution of charged residues (basic N-terminal acidic C-terminal halves). Yeast orthologues CHMPs, including an ESCRT-III component Snf7, are required for the sorting cargo proteins intraluminal vesicles bodies. We characterized novel human ESCRT-III-related protein, designated CHMP7, which consists 453 residues. CHMP7...
Exit of cargo molecules from the endoplasmic reticulum (ER) for transport to Golgi is initial step in intracellular vesicular trafficking. The coat protein complex II (COPII) machinery recruited specialized regions ER, called ER exit sites (ERES), where it plays a central role early secretory pathway. It has been known more than two decades that calcium an essential factor vesicle trafficking apparatus. However, pathway complicated and poorly understood. We others previously identified...
PKN, a novel protein kinase with catalytic domain homologous to that of the C (PKC) family and unique N-terminal leucine-zipper-like sequences, was identified by molecular cloning from human hippocampus cDNA library [Mukai Ono (1994) Biochem. Biophys. Res. Commun. 199, 897-904]. Recently we partially purified recombinant PKN COS7 cells transfected construct encoding demonstrated activated unsaturated fatty acids limited proteolysis [Mukai, Kitagawa, Shibata et al. 204, 348-356]. The present...
ALG-2 is a Ca(2+)-binding protein that belongs to the penta-EF-hand family and associates with several proteins, including annexin VII, XI, Alix/AIP1, in Ca(2+)-dependent manner. The yeast two-hybrid system biotin-tagged overlay assay were carried out characterize interaction between Alix. region corresponding amino acid residues 794 827 carboxy-terminal proline-rich of Alix was sufficient confer ability interact directly ALG-2. This includes four-tandem PxY repeats. Alanine substitutions...